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HEADER TRANSFERASE 04-SEP-07 2VAV
TITLE CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
TITLE 2 ACETYLTRANSFERASE (DAC-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 ACETYL TRANSFERASE, A/B- HYDROLASE FOLD, TRANSFERASE,
KEYWDS 2 ACYLTRANSFERASE, ACETYL COENZYME A, ANTIBIOTIC
KEYWDS 3 BIOSYNTHESIS, CEPHALOSPORIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEJON,J.ELLIS,K.VALEGARD
REVDAT 1 23-SEP-08 2VAV 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. 2.5 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 103.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.86
REMARK 3 NUMBER OF REFLECTIONS : 173708
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) : 0.21981
REMARK 3 R VALUE (WORKING SET) : 0.21908
REMARK 3 FREE R VALUE : 0.25482
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.9
REMARK 3 FREE R VALUE TEST SET COUNT : 3419
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) : 2.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.565
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13037
REMARK 3 BIN R VALUE (WORKING SET) : 0.295
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32530
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 519
REMARK 3 SOLVENT ATOMS : 499
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.519
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.95
REMARK 3 B22 (A**2) : 1.92
REMARK 3 B33 (A**2) : -0.97
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.11
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.508
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.526
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 33846 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 45904 ; 1.718 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4131 ; 7.269 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1623 ;31.398 ;22.693
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5315 ;16.719 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 323 ;19.365 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4903 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 26463 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 14673 ; 0.226 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 23459 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1301 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 258 ; 0.308 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 32 ; 0.326 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 21052 ; 0.967 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 33235 ; 1.573 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 14417 ; 2.405 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 12629 ; 3.951 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 16
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 32 1
REMARK 3 1 B 7 B 32 1
REMARK 3 1 C 7 C 32 1
REMARK 3 1 D 7 D 32 1
REMARK 3 1 E 7 E 32 1
REMARK 3 1 F 7 F 32 1
REMARK 3 1 G 7 G 32 1
REMARK 3 1 H 7 H 32 1
REMARK 3 1 I 7 I 32 1
REMARK 3 1 J 7 J 32 1
REMARK 3 1 K 7 K 32 1
REMARK 3 1 L 7 L 32 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 194 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 C (A): 194 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 D (A): 194 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 E (A): 194 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 F (A): 194 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 1 G (A): 194 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 H (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 I (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 J (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 K (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 L (A): 194 ; .06 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 194 ; .28 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 194 ; .31 ; .50
REMARK 3 TIGHT THERMAL 1 C (A**2): 194 ; .22 ; .50
REMARK 3 TIGHT THERMAL 1 D (A**2): 194 ; .22 ; .50
REMARK 3 TIGHT THERMAL 1 E (A**2): 194 ; .27 ; .50
REMARK 3 TIGHT THERMAL 1 F (A**2): 194 ; .25 ; .50
REMARK 3 TIGHT THERMAL 1 G (A**2): 194 ; .14 ; .50
REMARK 3 TIGHT THERMAL 1 H (A**2): 194 ; .13 ; .50
REMARK 3 TIGHT THERMAL 1 I (A**2): 194 ; .30 ; .50
REMARK 3 TIGHT THERMAL 1 J (A**2): 194 ; .49 ; .50
REMARK 3 TIGHT THERMAL 1 K (A**2): 194 ; .49 ; .50
REMARK 3 TIGHT THERMAL 1 L (A**2): 194 ; .25 ; .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 34 A 48 1
REMARK 3 1 B 34 B 48 1
REMARK 3 1 C 34 C 48 1
REMARK 3 1 D 34 D 48 1
REMARK 3 1 E 34 E 48 1
REMARK 3 1 F 34 F 48 1
REMARK 3 1 G 34 G 48 1
REMARK 3 1 H 34 H 48 1
REMARK 3 1 I 34 I 48 1
REMARK 3 1 J 34 J 48 1
REMARK 3 1 K 34 K 48 1
REMARK 3 1 L 34 L 48 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 119 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 B (A): 119 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 C (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 D (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 E (A): 119 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 F (A): 119 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 2 G (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 H (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 I (A): 119 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 J (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 K (A): 119 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 L (A): 119 ; .08 ; .05
REMARK 3 TIGHT THERMAL 2 A (A**2): 119 ; .19 ; .50
REMARK 3 TIGHT THERMAL 2 B (A**2): 119 ; .22 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 119 ; .25 ; .50
REMARK 3 TIGHT THERMAL 2 D (A**2): 119 ; .24 ; .50
REMARK 3 TIGHT THERMAL 2 E (A**2): 119 ; .19 ; .50
REMARK 3 TIGHT THERMAL 2 F (A**2): 119 ; .20 ; .50
REMARK 3 TIGHT THERMAL 2 G (A**2): 119 ; .21 ; .50
REMARK 3 TIGHT THERMAL 2 H (A**2): 119 ; .21 ; .50
REMARK 3 TIGHT THERMAL 2 I (A**2): 119 ; .20 ; .50
REMARK 3 TIGHT THERMAL 2 J (A**2): 119 ; .44 ; .50
REMARK 3 TIGHT THERMAL 2 K (A**2): 119 ; .44 ; .50
REMARK 3 TIGHT THERMAL 2 L (A**2): 119 ; .22 ; .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 50 A 119 1
REMARK 3 1 B 50 B 119 1
REMARK 3 1 C 50 C 119 1
REMARK 3 1 D 50 D 119 1
REMARK 3 1 E 50 E 119 1
REMARK 3 1 F 50 F 119 1
REMARK 3 1 G 50 G 119 1
REMARK 3 1 H 50 H 119 1
REMARK 3 1 I 50 I 119 1
REMARK 3 1 J 50 J 119 1
REMARK 3 1 K 50 K 119 1
REMARK 3 1 L 50 L 119 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 483 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 B (A): 483 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 C (A): 483 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 3 D (A): 483 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 3 E (A): 483 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 F (A): 483 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 G (A): 483 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 H (A): 483 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 I (A): 483 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 J (A): 483 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 3 K (A): 483 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 3 L (A): 483 ; .07 ; .05
REMARK 3 TIGHT THERMAL 3 A (A**2): 483 ; .19 ; .50
REMARK 3 TIGHT THERMAL 3 B (A**2): 483 ; .24 ; .50
REMARK 3 TIGHT THERMAL 3 C (A**2): 483 ; .24 ; .50
REMARK 3 TIGHT THERMAL 3 D (A**2): 483 ; .25 ; .50
REMARK 3 TIGHT THERMAL 3 E (A**2): 483 ; .19 ; .50
REMARK 3 TIGHT THERMAL 3 F (A**2): 483 ; .19 ; .50
REMARK 3 TIGHT THERMAL 3 G (A**2): 483 ; .17 ; .50
REMARK 3 TIGHT THERMAL 3 H (A**2): 483 ; .16 ; .50
REMARK 3 TIGHT THERMAL 3 I (A**2): 483 ; .24 ; .50
REMARK 3 TIGHT THERMAL 3 J (A**2): 483 ; .47 ; .50
REMARK 3 TIGHT THERMAL 3 K (A**2): 483 ; .47 ; .50
REMARK 3 TIGHT THERMAL 3 L (A**2): 483 ; .18 ; .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 121 A 127 1
REMARK 3 1 B 121 B 127 1
REMARK 3 1 C 121 C 127 1
REMARK 3 1 D 121 D 127 1
REMARK 3 1 E 121 E 127 1
REMARK 3 1 F 121 F 127 1
REMARK 3 1 G 121 G 127 1
REMARK 3 1 H 121 H 127 1
REMARK 3 1 I 121 I 127 1
REMARK 3 1 J 121 J 127 1
REMARK 3 1 K 121 K 127 1
REMARK 3 1 L 121 L 127 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 56 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 B (A): 56 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 C (A): 56 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 4 D (A): 56 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 4 E (A): 56 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 F (A): 56 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 G (A): 56 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 H (A): 56 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 I (A): 56 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 J (A): 56 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 4 K (A): 56 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 4 L (A): 56 ; .06 ; .05
REMARK 3 TIGHT THERMAL 4 A (A**2): 56 ; .34 ; .50
REMARK 3 TIGHT THERMAL 4 B (A**2): 56 ; .31 ; .50
REMARK 3 TIGHT THERMAL 4 C (A**2): 56 ; .30 ; .50
REMARK 3 TIGHT THERMAL 4 D (A**2): 56 ; .31 ; .50
REMARK 3 TIGHT THERMAL 4 E (A**2): 56 ; .32 ; .50
REMARK 3 TIGHT THERMAL 4 F (A**2): 56 ; .23 ; .50
REMARK 3 TIGHT THERMAL 4 G (A**2): 56 ; .19 ; .50
REMARK 3 TIGHT THERMAL 4 H (A**2): 56 ; .17 ; .50
REMARK 3 TIGHT THERMAL 4 I (A**2): 56 ; .34 ; .50
REMARK 3 TIGHT THERMAL 4 J (A**2): 56 ; .66 ; .50
REMARK 3 TIGHT THERMAL 4 K (A**2): 56 ; .70 ; .50
REMARK 3 TIGHT THERMAL 4 L (A**2): 56 ; .24 ; .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 129 A 130 1
REMARK 3 1 B 129 B 130 1
REMARK 3 1 C 129 C 130 1
REMARK 3 1 D 129 D 130 1
REMARK 3 1 E 129 E 130 1
REMARK 3 1 F 129 F 130 1
REMARK 3 1 G 129 G 130 1
REMARK 3 1 H 129 H 130 1
REMARK 3 1 I 129 I 130 1
REMARK 3 1 J 129 J 130 1
REMARK 3 1 K 129 K 130 1
REMARK 3 1 L 129 L 130 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 18 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 B (A): 18 ; .03 ; .05
REMARK 3 TIGHT POSITIONAL 5 C (A): 18 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 D (A): 18 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 E (A): 18 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 F (A): 18 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 5 G (A): 18 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 5 H (A): 18 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 5 I (A): 18 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 5 J (A): 18 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 5 K (A): 18 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 5 L (A): 18 ; .05 ; .05
REMARK 3 TIGHT THERMAL 5 A (A**2): 18 ; .26 ; .50
REMARK 3 TIGHT THERMAL 5 B (A**2): 18 ; .40 ; .50
REMARK 3 TIGHT THERMAL 5 C (A**2): 18 ; .38 ; .50
REMARK 3 TIGHT THERMAL 5 D (A**2): 18 ; .35 ; .50
REMARK 3 TIGHT THERMAL 5 E (A**2): 18 ; .31 ; .50
REMARK 3 TIGHT THERMAL 5 F (A**2): 18 ; .25 ; .50
REMARK 3 TIGHT THERMAL 5 G (A**2): 18 ; .23 ; .50
REMARK 3 TIGHT THERMAL 5 H (A**2): 18 ; .16 ; .50
REMARK 3 TIGHT THERMAL 5 I (A**2): 18 ; .38 ; .50
REMARK 3 TIGHT THERMAL 5 J (A**2): 18 ; .77 ; .50
REMARK 3 TIGHT THERMAL 5 K (A**2): 18 ; .77 ; .50
REMARK 3 TIGHT THERMAL 5 L (A**2): 18 ; .30 ; .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 132 A 139 1
REMARK 3 1 B 132 B 139 1
REMARK 3 1 C 132 C 139 1
REMARK 3 1 D 132 D 139 1
REMARK 3 1 E 132 E 139 1
REMARK 3 1 F 132 F 139 1
REMARK 3 1 G 132 G 139 1
REMARK 3 1 H 132 H 139 1
REMARK 3 1 I 132 I 139 1
REMARK 3 1 J 132 J 139 1
REMARK 3 1 K 132 K 139 1
REMARK 3 1 L 132 L 139 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 62 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 B (A): 62 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 C (A): 62 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 6 D (A): 62 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 E (A): 62 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 F (A): 62 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 6 G (A): 62 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 6 H (A): 62 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 I (A): 62 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 J (A): 62 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 K (A): 62 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 L (A): 62 ; .07 ; .05
REMARK 3 TIGHT THERMAL 6 A (A**2): 62 ; .19 ; .50
REMARK 3 TIGHT THERMAL 6 B (A**2): 62 ; .32 ; .50
REMARK 3 TIGHT THERMAL 6 C (A**2): 62 ; .22 ; .50
REMARK 3 TIGHT THERMAL 6 D (A**2): 62 ; .22 ; .50
REMARK 3 TIGHT THERMAL 6 E (A**2): 62 ; .20 ; .50
REMARK 3 TIGHT THERMAL 6 F (A**2): 62 ; .20 ; .50
REMARK 3 TIGHT THERMAL 6 G (A**2): 62 ; .13 ; .50
REMARK 3 TIGHT THERMAL 6 H (A**2): 62 ; .15 ; .50
REMARK 3 TIGHT THERMAL 6 I (A**2): 62 ; .30 ; .50
REMARK 3 TIGHT THERMAL 6 J (A**2): 62 ; .50 ; .50
REMARK 3 TIGHT THERMAL 6 K (A**2): 62 ; .50 ; .50
REMARK 3 TIGHT THERMAL 6 L (A**2): 62 ; .17 ; .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 141 A 144 1
REMARK 3 1 B 141 B 144 1
REMARK 3 1 C 141 C 144 1
REMARK 3 1 D 141 D 144 1
REMARK 3 1 E 141 E 144 1
REMARK 3 1 F 141 F 144 1
REMARK 3 1 G 141 G 144 1
REMARK 3 1 H 141 H 144 1
REMARK 3 1 I 141 I 144 1
REMARK 3 1 J 141 J 144 1
REMARK 3 1 K 141 K 144 1
REMARK 3 1 L 141 L 144 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 27 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 B (A): 27 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 7 C (A): 27 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 D (A): 27 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 E (A): 27 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 F (A): 27 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 7 G (A): 27 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 H (A): 27 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 I (A): 27 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 7 J (A): 27 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 K (A): 27 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 L (A): 27 ; .04 ; .05
REMARK 3 TIGHT THERMAL 7 A (A**2): 27 ; .17 ; .50
REMARK 3 TIGHT THERMAL 7 B (A**2): 27 ; .26 ; .50
REMARK 3 TIGHT THERMAL 7 C (A**2): 27 ; .21 ; .50
REMARK 3 TIGHT THERMAL 7 D (A**2): 27 ; .18 ; .50
REMARK 3 TIGHT THERMAL 7 E (A**2): 27 ; .19 ; .50
REMARK 3 TIGHT THERMAL 7 F (A**2): 27 ; .18 ; .50
REMARK 3 TIGHT THERMAL 7 G (A**2): 27 ; .19 ; .50
REMARK 3 TIGHT THERMAL 7 H (A**2): 27 ; .21 ; .50
REMARK 3 TIGHT THERMAL 7 I (A**2): 27 ; .24 ; .50
REMARK 3 TIGHT THERMAL 7 J (A**2): 27 ; .41 ; .50
REMARK 3 TIGHT THERMAL 7 K (A**2): 27 ; .46 ; .50
REMARK 3 TIGHT THERMAL 7 L (A**2): 27 ; .15 ; .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 146 A 189 1
REMARK 3 1 B 146 B 189 1
REMARK 3 1 C 146 C 189 1
REMARK 3 1 D 146 D 189 1
REMARK 3 1 E 146 E 189 1
REMARK 3 1 F 146 F 189 1
REMARK 3 1 G 146 G 189 1
REMARK 3 1 H 146 H 189 1
REMARK 3 1 I 146 I 189 1
REMARK 3 1 J 146 J 189 1
REMARK 3 1 K 146 K 189 1
REMARK 3 1 L 146 L 189 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 A (A): 350 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 B (A): 350 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 C (A): 350 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 D (A): 350 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 E (A): 350 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 F (A): 350 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 G (A): 350 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 8 H (A): 350 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 8 I (A): 350 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 J (A): 350 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 8 K (A): 350 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 8 L (A): 350 ; .06 ; .05
REMARK 3 TIGHT THERMAL 8 A (A**2): 350 ; .20 ; .50
REMARK 3 TIGHT THERMAL 8 B (A**2): 350 ; .25 ; .50
REMARK 3 TIGHT THERMAL 8 C (A**2): 350 ; .19 ; .50
REMARK 3 TIGHT THERMAL 8 D (A**2): 350 ; .18 ; .50
REMARK 3 TIGHT THERMAL 8 E (A**2): 350 ; .19 ; .50
REMARK 3 TIGHT THERMAL 8 F (A**2): 350 ; .17 ; .50
REMARK 3 TIGHT THERMAL 8 G (A**2): 350 ; .18 ; .50
REMARK 3 TIGHT THERMAL 8 H (A**2): 350 ; .19 ; .50
REMARK 3 TIGHT THERMAL 8 I (A**2): 350 ; .24 ; .50
REMARK 3 TIGHT THERMAL 8 J (A**2): 350 ; .47 ; .50
REMARK 3 TIGHT THERMAL 8 K (A**2): 350 ; .46 ; .50
REMARK 3 TIGHT THERMAL 8 L (A**2): 350 ; .18 ; .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 191 A 199 1
REMARK 3 1 B 191 B 199 1
REMARK 3 1 C 191 C 199 1
REMARK 3 1 D 191 D 199 1
REMARK 3 1 E 191 E 199 1
REMARK 3 1 F 191 F 199 1
REMARK 3 1 G 191 G 199 1
REMARK 3 1 H 191 H 199 1
REMARK 3 1 I 191 I 199 1
REMARK 3 1 J 191 J 199 1
REMARK 3 1 K 191 K 199 1
REMARK 3 1 L 191 L 199 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 A (A): 79 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 9 B (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 C (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 D (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 E (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 F (A): 79 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 G (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 H (A): 79 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 I (A): 79 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 J (A): 79 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 K (A): 79 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 L (A): 79 ; .05 ; .05
REMARK 3 TIGHT THERMAL 9 A (A**2): 79 ; .22 ; .50
REMARK 3 TIGHT THERMAL 9 B (A**2): 79 ; .20 ; .50
REMARK 3 TIGHT THERMAL 9 C (A**2): 79 ; .16 ; .50
REMARK 3 TIGHT THERMAL 9 D (A**2): 79 ; .15 ; .50
REMARK 3 TIGHT THERMAL 9 E (A**2): 79 ; .21 ; .50
REMARK 3 TIGHT THERMAL 9 F (A**2): 79 ; .17 ; .50
REMARK 3 TIGHT THERMAL 9 G (A**2): 79 ; .13 ; .50
REMARK 3 TIGHT THERMAL 9 H (A**2): 79 ; .14 ; .50
REMARK 3 TIGHT THERMAL 9 I (A**2): 79 ; .21 ; .50
REMARK 3 TIGHT THERMAL 9 J (A**2): 79 ; .33 ; .50
REMARK 3 TIGHT THERMAL 9 K (A**2): 79 ; .33 ; .50
REMARK 3 TIGHT THERMAL 9 L (A**2): 79 ; .17 ; .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 202 A 217 1
REMARK 3 1 B 202 B 217 1
REMARK 3 1 C 202 C 217 1
REMARK 3 1 D 202 D 217 1
REMARK 3 1 E 202 E 217 1
REMARK 3 1 F 202 F 217 1
REMARK 3 1 G 202 G 217 1
REMARK 3 1 H 202 H 217 1
REMARK 3 1 I 202 I 217 1
REMARK 3 1 J 202 J 217 1
REMARK 3 1 K 202 K 217 1
REMARK 3 1 L 202 L 217 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 A (A): 123 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 B (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 C (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 D (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 E (A): 123 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 F (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 G (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 H (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 I (A): 123 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 J (A): 123 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 K (A): 123 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 L (A): 123 ; .04 ; .05
REMARK 3 TIGHT THERMAL 10 A (A**2): 123 ; .14 ; .50
REMARK 3 TIGHT THERMAL 10 B (A**2): 123 ; .17 ; .50
REMARK 3 TIGHT THERMAL 10 C (A**2): 123 ; .13 ; .50
REMARK 3 TIGHT THERMAL 10 D (A**2): 123 ; .12 ; .50
REMARK 3 TIGHT THERMAL 10 E (A**2): 123 ; .20 ; .50
REMARK 3 TIGHT THERMAL 10 F (A**2): 123 ; .12 ; .50
REMARK 3 TIGHT THERMAL 10 G (A**2): 123 ; .13 ; .50
REMARK 3 TIGHT THERMAL 10 H (A**2): 123 ; .12 ; .50
REMARK 3 TIGHT THERMAL 10 I (A**2): 123 ; .18 ; .50
REMARK 3 TIGHT THERMAL 10 J (A**2): 123 ; .24 ; .50
REMARK 3 TIGHT THERMAL 10 K (A**2): 123 ; .24 ; .50
REMARK 3 TIGHT THERMAL 10 L (A**2): 123 ; .13 ; .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 219 A 237 1
REMARK 3 1 B 219 B 237 1
REMARK 3 1 C 219 C 237 1
REMARK 3 1 D 219 D 237 1
REMARK 3 1 E 219 E 237 1
REMARK 3 1 F 219 F 237 1
REMARK 3 1 G 219 G 237 1
REMARK 3 1 H 219 H 237 1
REMARK 3 1 I 219 I 237 1
REMARK 3 1 J 219 J 237 1
REMARK 3 1 K 219 K 237 1
REMARK 3 1 L 219 L 237 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 A (A): 158 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 11 B (A): 158 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 C (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 D (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 E (A): 158 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 11 F (A): 158 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 11 G (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 H (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 I (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 J (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 K (A): 158 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 L (A): 158 ; .06 ; .05
REMARK 3 TIGHT THERMAL 11 A (A**2): 158 ; .21 ; .50
REMARK 3 TIGHT THERMAL 11 B (A**2): 158 ; .19 ; .50
REMARK 3 TIGHT THERMAL 11 C (A**2): 158 ; .26 ; .50
REMARK 3 TIGHT THERMAL 11 D (A**2): 158 ; .25 ; .50
REMARK 3 TIGHT THERMAL 11 E (A**2): 158 ; .19 ; .50
REMARK 3 TIGHT THERMAL 11 F (A**2): 158 ; .17 ; .50
REMARK 3 TIGHT THERMAL 11 G (A**2): 158 ; .15 ; .50
REMARK 3 TIGHT THERMAL 11 H (A**2): 158 ; .15 ; .50
REMARK 3 TIGHT THERMAL 11 I (A**2): 158 ; .21 ; .50
REMARK 3 TIGHT THERMAL 11 J (A**2): 158 ; .17 ; .50
REMARK 3 TIGHT THERMAL 11 K (A**2): 158 ; .16 ; .50
REMARK 3 TIGHT THERMAL 11 L (A**2): 158 ; .17 ; .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 270 A 303 1
REMARK 3 1 B 270 B 303 1
REMARK 3 1 C 270 C 303 1
REMARK 3 1 D 270 D 303 1
REMARK 3 1 E 270 E 303 1
REMARK 3 1 F 270 F 303 1
REMARK 3 1 G 270 G 303 1
REMARK 3 1 H 270 H 303 1
REMARK 3 1 I 270 I 303 1
REMARK 3 1 J 270 J 303 1
REMARK 3 1 K 270 K 303 1
REMARK 3 1 L 270 L 303 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 A (A): 271 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 12 B (A): 271 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 12 C (A): 271 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 D (A): 271 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 E (A): 271 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 12 F (A): 271 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 12 G (A): 271 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 H (A): 271 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 I (A): 271 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 12 J (A): 271 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 12 K (A): 271 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 12 L (A): 271 ; .07 ; .05
REMARK 3 TIGHT THERMAL 12 A (A**2): 271 ; .19 ; .50
REMARK 3 TIGHT THERMAL 12 B (A**2): 271 ; .22 ; .50
REMARK 3 TIGHT THERMAL 12 C (A**2): 271 ; .20 ; .50
REMARK 3 TIGHT THERMAL 12 D (A**2): 271 ; .21 ; .50
REMARK 3 TIGHT THERMAL 12 E (A**2): 271 ; .19 ; .50
REMARK 3 TIGHT THERMAL 12 F (A**2): 271 ; .18 ; .50
REMARK 3 TIGHT THERMAL 12 G (A**2): 271 ; .15 ; .50
REMARK 3 TIGHT THERMAL 12 H (A**2): 271 ; .14 ; .50
REMARK 3 TIGHT THERMAL 12 I (A**2): 271 ; .22 ; .50
REMARK 3 TIGHT THERMAL 12 J (A**2): 271 ; .35 ; .50
REMARK 3 TIGHT THERMAL 12 K (A**2): 271 ; .36 ; .50
REMARK 3 TIGHT THERMAL 12 L (A**2): 271 ; .17 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
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 304 A 307 1
REMARK 3 1 B 304 B 307 1
REMARK 3 1 C 304 C 307 1
REMARK 3 1 D 304 D 307 1
REMARK 3 1 E 304 E 307 1
REMARK 3 1 F 304 F 307 1
REMARK 3 1 G 304 G 307 1
REMARK 3 1 H 304 H 307 1
REMARK 3 1 I 304 I 307 1
REMARK 3 1 J 304 J 307 1
REMARK 3 1 K 304 K 307 1
REMARK 3 1 L 304 L 307 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 13 A (A): 32 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 13 B (A): 32 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 13 C (A): 32 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 13 D (A): 32 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 13 E (A): 32 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 13 F (A): 32 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 13 G (A): 32 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 13 H (A): 32 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 13 I (A): 32 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 13 J (A): 32 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 13 K (A): 32 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 13 L (A): 32 ; .06 ; .05
REMARK 3 TIGHT THERMAL 13 A (A**2): 32 ; .27 ; .50
REMARK 3 TIGHT THERMAL 13 B (A**2): 32 ; .29 ; .50
REMARK 3 TIGHT THERMAL 13 C (A**2): 32 ; .23 ; .50
REMARK 3 TIGHT THERMAL 13 D (A**2): 32 ; .22 ; .50
REMARK 3 TIGHT THERMAL 13 E (A**2): 32 ; .26 ; .50
REMARK 3 TIGHT THERMAL 13 F (A**2): 32 ; .19 ; .50
REMARK 3 TIGHT THERMAL 13 G (A**2): 32 ; .13 ; .50
REMARK 3 TIGHT THERMAL 13 H (A**2): 32 ; .12 ; .50
REMARK 3 TIGHT THERMAL 13 I (A**2): 32 ; .34 ; .50
REMARK 3 TIGHT THERMAL 13 J (A**2): 32 ; .55 ; .50
REMARK 3 TIGHT THERMAL 13 K (A**2): 32 ; .57 ; .50
REMARK 3 TIGHT THERMAL 13 L (A**2): 32 ; .19 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
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 14 A (A): 151 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 14 B (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 C (A): 151 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 14 D (A): 151 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 14 E (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 F (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 14 G (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 H (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 I (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 14 J (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 K (A): 151 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 14 L (A): 151 ; .06 ; .05
REMARK 3 TIGHT THERMAL 14 A (A**2): 151 ; .19 ; .50
REMARK 3 TIGHT THERMAL 14 B (A**2): 151 ; .23 ; .50
REMARK 3 TIGHT THERMAL 14 C (A**2): 151 ; .18 ; .50
REMARK 3 TIGHT THERMAL 14 D (A**2): 151 ; .17 ; .50
REMARK 3 TIGHT THERMAL 14 E (A**2): 151 ; .18 ; .50
REMARK 3 TIGHT THERMAL 14 F (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 14 G (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 14 H (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 14 I (A**2): 151 ; .23 ; .50
REMARK 3 TIGHT THERMAL 14 J (A**2): 151 ; .39 ; .50
REMARK 3 TIGHT THERMAL 14 K (A**2): 151 ; .41 ; .50
REMARK 3 TIGHT THERMAL 14 L (A**2): 151 ; .15 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
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 359 1
REMARK 3 1 B 332 B 359 1
REMARK 3 1 C 332 C 359 1
REMARK 3 1 D 332 D 359 1
REMARK 3 1 E 332 E 359 1
REMARK 3 1 F 332 F 359 1
REMARK 3 1 G 332 G 359 1
REMARK 3 1 H 332 H 359 1
REMARK 3 1 I 332 I 359 1
REMARK 3 1 J 332 J 359 1
REMARK 3 1 K 332 K 359 1
REMARK 3 1 L 332 L 359 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 15 A (A): 210 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 15 B (A): 210 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 15 C (A): 210 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 15 D (A): 210 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 15 E (A): 210 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 15 F (A): 210 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 15 G (A): 210 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 15 H (A): 210 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 15 I (A): 210 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 15 J (A): 210 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 15 K (A): 210 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 15 L (A): 210 ; .07 ; .05
REMARK 3 TIGHT THERMAL 15 A (A**2): 210 ; .14 ; .50
REMARK 3 TIGHT THERMAL 15 B (A**2): 210 ; .18 ; .50
REMARK 3 TIGHT THERMAL 15 C (A**2): 210 ; .15 ; .50
REMARK 3 TIGHT THERMAL 15 D (A**2): 210 ; .15 ; .50
REMARK 3 TIGHT THERMAL 15 E (A**2): 210 ; .14 ; .50
REMARK 3 TIGHT THERMAL 15 F (A**2): 210 ; .17 ; .50
REMARK 3 TIGHT THERMAL 15 G (A**2): 210 ; .15 ; .50
REMARK 3 TIGHT THERMAL 15 H (A**2): 210 ; .14 ; .50
REMARK 3 TIGHT THERMAL 15 I (A**2): 210 ; .17 ; .50
REMARK 3 TIGHT THERMAL 15 J (A**2): 210 ; .28 ; .50
REMARK 3 TIGHT THERMAL 15 K (A**2): 210 ; .29 ; .50
REMARK 3 TIGHT THERMAL 15 L (A**2): 210 ; .16 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 361 A 382 1
REMARK 3 1 B 361 B 382 1
REMARK 3 1 C 361 C 382 1
REMARK 3 1 D 361 D 382 1
REMARK 3 1 E 361 E 382 1
REMARK 3 1 F 361 F 382 1
REMARK 3 1 G 361 G 382 1
REMARK 3 1 H 361 H 382 1
REMARK 3 1 I 361 I 382 1
REMARK 3 1 J 361 J 382 1
REMARK 3 1 K 361 K 382 1
REMARK 3 1 L 361 L 382 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 16 A (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 B (A): 176 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 16 C (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 D (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 E (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 F (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 G (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 H (A): 176 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 16 I (A): 176 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 16 J (A): 176 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 16 K (A): 176 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 16 L (A): 176 ; .06 ; .05
REMARK 3 TIGHT THERMAL 16 A (A**2): 176 ; .13 ; .50
REMARK 3 TIGHT THERMAL 16 B (A**2): 176 ; .21 ; .50
REMARK 3 TIGHT THERMAL 16 C (A**2): 176 ; .15 ; .50
REMARK 3 TIGHT THERMAL 16 D (A**2): 176 ; .14 ; .50
REMARK 3 TIGHT THERMAL 16 E (A**2): 176 ; .14 ; .50
REMARK 3 TIGHT THERMAL 16 F (A**2): 176 ; .17 ; .50
REMARK 3 TIGHT THERMAL 16 G (A**2): 176 ; .14 ; .50
REMARK 3 TIGHT THERMAL 16 H (A**2): 176 ; .14 ; .50
REMARK 3 TIGHT THERMAL 16 I (A**2): 176 ; .20 ; .50
REMARK 3 TIGHT THERMAL 16 J (A**2): 176 ; .27 ; .50
REMARK 3 TIGHT THERMAL 16 K (A**2): 176 ; .27 ; .50
REMARK 3 TIGHT THERMAL 16 L (A**2): 176 ; .17 ; .50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. RESIDUES 242-267 ARE DISORDERED.
REMARK 3 CEPHALOSPORIN C WAS MODELLED IN MULTIPLE CONFORMATIONS.
REMARK 3 ACETYLSERINE WAS MODELLED IN MULTIPLE CONFORMATIONS.
REMARK 4
REMARK 4 2VAV 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-33687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177299
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 109.11
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.7
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.37
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.30
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 (%): 52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
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 54.43250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 7 .. 382 A 7 .. 382 0.329
REMARK 295 M 2 C 7 .. 382 A 7 .. 382 0.511
REMARK 295 M 3 D 7 .. 382 A 7 .. 382 0.435
REMARK 295 M 4 E 7 .. 382 A 7 .. 382 0.133
REMARK 295 M 5 F 7 .. 382 A 7 .. 382 0.493
REMARK 295 M 6 G 7 .. 382 A 7 .. 382 0.552
REMARK 295 M 7 H 7 .. 382 A 7 .. 382 0.650
REMARK 295 M 8 I 7 .. 382 A 7 .. 382 0.300
REMARK 295 M 9 J 7 .. 382 A 7 .. 382 0.531
REMARK 295 M 10 K 7 .. 382 A 7 .. 382 0.517
REMARK 295 M 11 L 7 .. 382 A 7 .. 382 0.467
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: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.1 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: 5210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.2 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: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.5 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: 3640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.7 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: 4110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.4 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: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -58
REMARK 465 LEU A -57
REMARK 465 PRO A -56
REMARK 465 SER A -55
REMARK 465 ALA A -54
REMARK 465 GLN A -53
REMARK 465 VAL A -52
REMARK 465 ALA A -51
REMARK 465 ARG A -50
REMARK 465 LEU A -49
REMARK 465 LYS A -48
REMARK 465 PRO A -47
REMARK 465 ASP A -46
REMARK 465 PRO A -45
REMARK 465 PHE A -44
REMARK 465 PRO A -43
REMARK 465 PRO A -42
REMARK 465 SER A -41
REMARK 465 LEU A -40
REMARK 465 SER A -39
REMARK 465 PRO A -38
REMARK 465 ILE A -37
REMARK 465 PRO A -36
REMARK 465 HIS A -35
REMARK 465 GLY A -34
REMARK 465 ALA A -33
REMARK 465 VAL A -32
REMARK 465 THR A -31
REMARK 465 PHE A -30
REMARK 465 ALA A -29
REMARK 465 ALA A -28
REMARK 465 LEU A -27
REMARK 465 ALA A -26
REMARK 465 PRO A -25
REMARK 465 CYS A -24
REMARK 465 HIS A -23
REMARK 465 ASN A -22
REMARK 465 LEU A -21
REMARK 465 PRO A -20
REMARK 465 ILE A -19
REMARK 465 PHE A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 ARG A -15
REMARK 465 GLN A -14
REMARK 465 MET A -13
REMARK 465 LEU A -12
REMARK 465 ARG A -11
REMARK 465 ASP A -10
REMARK 465 SER A -9
REMARK 465 LEU A -8
REMARK 465 THR A -7
REMARK 465 TYR A -6
REMARK 465 SER A -5
REMARK 465 HIS A -4
REMARK 465 THR A -3
REMARK 465 SER A -2
REMARK 465 PRO A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 ILE A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 110
REMARK 465 GLN A 111
REMARK 465 GLN A 242
REMARK 465 ALA A 243
REMARK 465 GLY A 244
REMARK 465 ARG A 245
REMARK 465 ASN A 246
REMARK 465 ILE A 247
REMARK 465 SER A 248
REMARK 465 SER A 249
REMARK 465 GLN A 250
REMARK 465 ASP A 251
REMARK 465 ALA A 252
REMARK 465 LYS A 253
REMARK 465 LYS A 254
REMARK 465 GLU A 255
REMARK 465 ILE A 256
REMARK 465 ASN A 257
REMARK 465 GLY A 258
REMARK 465 THR A 259
REMARK 465 ASP A 260
REMARK 465 SER A 261
REMARK 465 GLY A 262
REMARK 465 ASN A 263
REMARK 465 SER A 264
REMARK 465 HIS A 265
REMARK 465 ARG A 266
REMARK 465 ALA A 267
REMARK 465 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 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 GLN C 4
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 SER F 383
REMARK 465 LEU F 384
REMARK 465 MET F 385
REMARK 465 MET G -58
REMARK 465 LEU G -57
REMARK 465 PRO G -56
REMARK 465 SER G -55
REMARK 465 ALA G -54
REMARK 465 GLN G -53
REMARK 465 VAL G -52
REMARK 465 ALA G -51
REMARK 465 ARG G -50
REMARK 465 LEU G -49
REMARK 465 LYS G -48
REMARK 465 PRO G -47
REMARK 465 ASP G -46
REMARK 465 PRO G -45
REMARK 465 PHE G -44
REMARK 465 PRO G -43
REMARK 465 PRO G -42
REMARK 465 SER G -41
REMARK 465 LEU G -40
REMARK 465 SER G -39
REMARK 465 PRO G -38
REMARK 465 ILE G -37
REMARK 465 PRO G -36
REMARK 465 HIS G -35
REMARK 465 GLY G -34
REMARK 465 ALA G -33
REMARK 465 VAL G -32
REMARK 465 THR G -31
REMARK 465 PHE G -30
REMARK 465 ALA G -29
REMARK 465 ALA G -28
REMARK 465 LEU G -27
REMARK 465 ALA G -26
REMARK 465 PRO G -25
REMARK 465 CYS G -24
REMARK 465 HIS G -23
REMARK 465 ASN G -22
REMARK 465 LEU G -21
REMARK 465 PRO G -20
REMARK 465 ILE G -19
REMARK 465 PHE G -18
REMARK 465 SER G -17
REMARK 465 SER G -16
REMARK 465 ARG G -15
REMARK 465 GLN G -14
REMARK 465 MET G -13
REMARK 465 LEU G -12
REMARK 465 ARG G -11
REMARK 465 ASP G -10
REMARK 465 SER G -9
REMARK 465 LEU G -8
REMARK 465 THR G -7
REMARK 465 TYR G -6
REMARK 465 SER G -5
REMARK 465 HIS G -4
REMARK 465 THR G -3
REMARK 465 SER G -2
REMARK 465 PRO G -1
REMARK 465 THR G 0
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 PRO G 3
REMARK 465 GLN G 4
REMARK 465 ILE G 5
REMARK 465 ALA G 6
REMARK 465 GLU G 109
REMARK 465 GLY G 110
REMARK 465 GLN G 111
REMARK 465 ALA G 238
REMARK 465 PRO G 239
REMARK 465 GLY G 240
REMARK 465 VAL G 241
REMARK 465 GLN G 242
REMARK 465 ALA G 243
REMARK 465 GLY G 244
REMARK 465 ARG G 245
REMARK 465 ASN G 246
REMARK 465 ILE G 247
REMARK 465 SER G 248
REMARK 465 SER G 249
REMARK 465 GLN G 250
REMARK 465 ASP G 251
REMARK 465 ALA G 252
REMARK 465 LYS G 253
REMARK 465 LYS G 254
REMARK 465 GLU G 255
REMARK 465 ILE G 256
REMARK 465 ASN G 257
REMARK 465 GLY G 258
REMARK 465 THR G 259
REMARK 465 ASP G 260
REMARK 465 SER G 261
REMARK 465 GLY G 262
REMARK 465 ASN G 263
REMARK 465 SER G 264
REMARK 465 HIS G 265
REMARK 465 ARG G 266
REMARK 465 ALA G 267
REMARK 465 GLY G 268
REMARK 465 SER G 383
REMARK 465 LEU G 384
REMARK 465 MET G 385
REMARK 465 MET H -58
REMARK 465 LEU H -57
REMARK 465 PRO H -56
REMARK 465 SER H -55
REMARK 465 ALA H -54
REMARK 465 GLN H -53
REMARK 465 VAL H -52
REMARK 465 ALA H -51
REMARK 465 ARG H -50
REMARK 465 LEU H -49
REMARK 465 LYS H -48
REMARK 465 PRO H -47
REMARK 465 ASP H -46
REMARK 465 PRO H -45
REMARK 465 PHE H -44
REMARK 465 PRO H -43
REMARK 465 PRO H -42
REMARK 465 SER H -41
REMARK 465 LEU H -40
REMARK 465 SER H -39
REMARK 465 PRO H -38
REMARK 465 ILE H -37
REMARK 465 PRO H -36
REMARK 465 HIS H -35
REMARK 465 GLY H -34
REMARK 465 ALA H -33
REMARK 465 VAL H -32
REMARK 465 THR H -31
REMARK 465 PHE H -30
REMARK 465 ALA H -29
REMARK 465 ALA H -28
REMARK 465 LEU H -27
REMARK 465 ALA H -26
REMARK 465 PRO H -25
REMARK 465 CYS H -24
REMARK 465 HIS H -23
REMARK 465 ASN H -22
REMARK 465 LEU H -21
REMARK 465 PRO H -20
REMARK 465 ILE H -19
REMARK 465 PHE H -18
REMARK 465 SER H -17
REMARK 465 SER H -16
REMARK 465 ARG H -15
REMARK 465 GLN H -14
REMARK 465 MET H -13
REMARK 465 LEU H -12
REMARK 465 ARG H -11
REMARK 465 ASP H -10
REMARK 465 SER H -9
REMARK 465 LEU H -8
REMARK 465 THR H -7
REMARK 465 TYR H -6
REMARK 465 SER H -5
REMARK 465 HIS H -4
REMARK 465 THR H -3
REMARK 465 SER H -2
REMARK 465 PRO H -1
REMARK 465 THR H 0
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 ILE H 5
REMARK 465 ALA H 6
REMARK 465 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 ALA I 6
REMARK 465 GLU I 109
REMARK 465 GLY I 110
REMARK 465 GLN I 111
REMARK 465 GLN I 242
REMARK 465 ALA I 243
REMARK 465 GLY I 244
REMARK 465 ARG I 245
REMARK 465 ASN I 246
REMARK 465 ILE I 247
REMARK 465 SER I 248
REMARK 465 SER I 249
REMARK 465 GLN I 250
REMARK 465 ASP I 251
REMARK 465 ALA I 252
REMARK 465 LYS I 253
REMARK 465 LYS I 254
REMARK 465 GLU I 255
REMARK 465 ILE I 256
REMARK 465 ASN I 257
REMARK 465 GLY I 258
REMARK 465 THR I 259
REMARK 465 ASP I 260
REMARK 465 SER I 261
REMARK 465 GLY I 262
REMARK 465 ASN I 263
REMARK 465 SER I 264
REMARK 465 HIS I 265
REMARK 465 ARG I 266
REMARK 465 ALA I 267
REMARK 465 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 PRO K 106
REMARK 465 ASP K 107
REMARK 465 ALA K 108
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 GLY L 268
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 ASP H 333 OD1 OD2
REMARK 470 SER I 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 O GLU B 10 - NH1 ARG F 44 2.07
REMARK 500 NH2 ARG F 346 - O HOH F 2038 2.15
REMARK 500 O GLU I 10 - NH1 ARG L 44 2.04
REMARK 500 NH1 ARG J 140 - O HOH J 2002 1.79
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 OE1 GLN G 283 NH2 ARG J 49 1656 2.11
REMARK 500 OE1 GLN H 283 NH2 ARG K 49 1755 2.02
REMARK 500 NH2 ARG J 49 OE1 GLN G 283 1646 2.11
REMARK 500 NH2 ARG K 49 OE1 GLN H 283 1745 2.02
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 CYS F 176 CB CYS F 176 SG -0.114
REMARK 500 CYS L 176 CB CYS L 176 SG -0.105
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 B 113 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG B 310 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 310 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG D 310 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG D 310 NE - CZ - NH2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 LEU G 134 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO I 113 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG K 140 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 144 148.25 -172.79
REMARK 500 ALA A 173 71.81 46.99
REMARK 500 GLN A 269 -44.23 -130.53
REMARK 500 ASP A 305 109.20 -168.72
REMARK 500 ASN A 350 68.28 -107.96
REMARK 500 ASP A 363 -30.07 -27.63
REMARK 500 PRO B 239 159.10 -49.99
REMARK 500 ASP B 305 106.83 -171.26
REMARK 500 ASN B 350 72.79 -110.59
REMARK 500 ASP B 363 -31.21 -28.11
REMARK 500 ASP C 107 -0.04 -57.69
REMARK 500 ALA C 173 70.69 47.62
REMARK 500 TYR C 204 156.81 -49.79
REMARK 500 ASP C 305 109.30 -166.00
REMARK 500 ASN C 350 71.59 -107.53
REMARK 500 ASP C 363 -30.52 -29.45
REMARK 500 ASP D 107 50.37 -63.51
REMARK 500 ALA D 173 70.49 49.03
REMARK 500 ASP D 305 107.97 -167.62
REMARK 500 ASN D 350 71.17 -107.87
REMARK 500 ASP D 363 -30.54 -26.59
REMARK 500 ALA E 144 148.20 -170.28
REMARK 500 ALA E 173 72.40 44.35
REMARK 500 GLN E 269 -45.52 -132.02
REMARK 500 ASP E 305 108.60 -168.22
REMARK 500 ASN E 350 70.07 -108.03
REMARK 500 ASP E 363 -27.29 -31.63
REMARK 500 ASP F 107 48.88 -84.97
REMARK 500 ASP F 305 108.51 -169.03
REMARK 500 ASN F 350 73.26 -108.10
REMARK 500 ASP F 363 -33.83 -26.14
REMARK 500 ASP G 305 109.84 -169.36
REMARK 500 ASN G 350 73.29 -105.83
REMARK 500 ASP G 363 -29.12 -29.12
REMARK 500 ASP H 305 109.44 -168.65
REMARK 500 ASN H 350 70.19 -105.15
REMARK 500 ASP H 363 -29.40 -28.73
REMARK 500 ALA I 173 70.53 45.45
REMARK 500 ASP I 201 27.12 49.77
REMARK 500 PRO I 239 155.54 -48.60
REMARK 500 ASP I 305 108.04 -172.52
REMARK 500 ASN I 350 72.94 -110.12
REMARK 500 ASP I 363 -32.22 -26.85
REMARK 500 ASP J 14 -179.70 -67.18
REMARK 500 PRO J 101 -19.14 -50.00
REMARK 500 ALA J 173 76.59 45.41
REMARK 500 LEU J 200 33.11 71.95
REMARK 500 SER J 288 37.21 -140.51
REMARK 500 ASP J 305 108.34 -168.48
REMARK 500 ASN J 350 68.11 -106.77
REMARK 500 ASP J 363 -30.91 -26.75
REMARK 500 ALA K 173 73.76 49.25
REMARK 500 ASP K 201 11.27 59.91
REMARK 500 ASP K 305 110.28 -173.47
REMARK 500 SER K 332 30.01 -99.48
REMARK 500 ASN K 350 68.74 -105.74
REMARK 500 ASP K 363 -31.84 -21.60
REMARK 500 ASP L 14 -179.39 -65.05
REMARK 500 ALA L 173 70.63 45.05
REMARK 500 ASP L 305 109.86 -167.69
REMARK 500 ASN L 350 74.43 -108.05
REMARK 500 ASP L 363 -32.56 -28.21
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 F 1383
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 G 1383
REMARK 610 CSC H 1383
REMARK 610 CSC I 1383
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 CSC B 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC C 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC D 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC E 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC F 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC G 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC H 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC I 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC J 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC K 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC L 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1386
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1386
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: 2VAX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
REMARK 900 ACETYLTRANSFERASE (COMPLEX II)
DBREF 2VAV A -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV B -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV C -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV D -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV E -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV F -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV G -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV H -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV I -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV J -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV K -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAV 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 2VAV OAS A 149 SER O-ACETYLSERINE
MODRES 2VAV OAS B 149 SER O-ACETYLSERINE
MODRES 2VAV OAS C 149 SER O-ACETYLSERINE
MODRES 2VAV OAS D 149 SER O-ACETYLSERINE
MODRES 2VAV OAS E 149 SER O-ACETYLSERINE
MODRES 2VAV OAS F 149 SER O-ACETYLSERINE
MODRES 2VAV OAS G 149 SER O-ACETYLSERINE
MODRES 2VAV OAS H 149 SER O-ACETYLSERINE
MODRES 2VAV OAS I 149 SER O-ACETYLSERINE
MODRES 2VAV OAS J 149 SER O-ACETYLSERINE
MODRES 2VAV OAS K 149 SER O-ACETYLSERINE
MODRES 2VAV OAS L 149 SER O-ACETYLSERINE
HET OAS A 149 12
HET OAS B 149 12
HET OAS C 149 12
HET OAS D 149 12
HET OAS E 149 12
HET OAS F 149 12
HET OAS G 149 12
HET OAS H 149 12
HET OAS I 149 12
HET OAS J 149 12
HET OAS K 149 12
HET OAS L 149 12
HET CSC A1383 25
HET CSC B1384 25
HET CSC C1383 25
HET CSC D1383 25
HET CSC E1383 25
HET CSC F1383 30
HET CSC G1383 25
HET CSC H1383 30
HET CSC I1383 25
HET CSC J1385 25
HET CSC K1385 25
HET CSC L1383 30
HET ACT A1384 4
HET ACT B1385 4
HET ACT E1384 4
HET ACT I1384 4
HET ACT H1384 4
HET ACT G1384 4
HET ACT D1384 4
HET ACT F1384 4
HET ACT C1384 4
HET ACT L1384 4
HET ACT B1386 4
HET ACT A1385 4
HET ACT E1385 4
HET ACT I1385 4
HET ACT I1386 4
HETNAM ACT ACETATE ION
HETNAM OAS O-ACETYLSERINE
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
FORMUL 13 ACT 15(C2 H3 O2 1-)
FORMUL 14 CSC 12(C16 H22 N3 O8 S)
FORMUL 15 OAS 12(C5 H9 N O4)
FORMUL 16 HOH *499(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 ASP A 105 GLU A 109 5 5
HELIX 5 5 TYR A 114 PHE A 118 5 5
HELIX 6 6 THR A 122 GLY A 138 1 17
HELIX 7 7 MET A 150 ALA A 159 1 10
HELIX 8 8 PHE A 160 GLY A 162 5 3
HELIX 9 9 SER A 179 ASP A 195 1 17
HELIX 10 10 TYR A 199 GLU A 203 5 5
HELIX 11 11 PRO A 210 TYR A 225 1 16
HELIX 12 12 SER A 227 PHE A 235 1 9
HELIX 13 13 ALA A 273 SER A 288 1 16
HELIX 14 14 ASP A 290 ASP A 302 1 13
HELIX 15 15 SER A 313 ALA A 319 1 7
HELIX 16 16 SER A 337 ILE A 348 1 12
HELIX 17 17 ASP A 363 GLU A 368 1 6
HELIX 18 18 GLU A 368 GLN A 382 1 15
HELIX 19 19 ASN B 7 SER B 12 1 6
HELIX 20 20 HIS B 64 TRP B 68 5 5
HELIX 21 21 TRP B 69 LEU B 72 5 4
HELIX 22 22 TYR B 114 PHE B 118 5 5
HELIX 23 23 THR B 122 GLY B 138 1 17
HELIX 24 24 MET B 150 ALA B 159 1 10
HELIX 25 25 PHE B 160 GLY B 162 5 3
HELIX 26 26 SER B 179 ASP B 195 1 17
HELIX 27 27 TYR B 199 GLU B 203 5 5
HELIX 28 28 PRO B 210 TYR B 225 1 16
HELIX 29 29 SER B 227 PHE B 235 1 9
HELIX 30 30 ALA B 273 SER B 288 1 16
HELIX 31 31 ASP B 290 PHE B 301 1 12
HELIX 32 32 ASP B 302 HIS B 304 5 3
HELIX 33 33 SER B 313 ALA B 319 1 7
HELIX 34 34 SER B 337 ILE B 348 1 12
HELIX 35 35 ASP B 363 GLU B 368 1 6
HELIX 36 36 GLU B 368 GLN B 382 1 15
HELIX 37 37 ASN C 7 SER C 12 1 6
HELIX 38 38 HIS C 64 TRP C 68 5 5
HELIX 39 39 TRP C 69 LEU C 72 5 4
HELIX 40 40 ASP C 105 GLU C 109 5 5
HELIX 41 41 TYR C 114 PHE C 118 5 5
HELIX 42 42 THR C 122 GLY C 138 1 17
HELIX 43 43 MET C 150 ALA C 159 1 10
HELIX 44 44 PHE C 160 GLY C 162 5 3
HELIX 45 45 SER C 179 ASP C 195 1 17
HELIX 46 46 TYR C 199 GLU C 203 5 5
HELIX 47 47 PRO C 210 TYR C 225 1 16
HELIX 48 48 SER C 227 PHE C 235 1 9
HELIX 49 49 ALA C 273 SER C 288 1 16
HELIX 50 50 ASP C 290 THR C 303 1 14
HELIX 51 51 SER C 313 ALA C 319 1 7
HELIX 52 52 SER C 337 ILE C 348 1 12
HELIX 53 53 ASP C 363 GLU C 368 1 6
HELIX 54 54 GLU C 368 GLN C 382 1 15
HELIX 55 55 ASN D 7 SER D 12 1 6
HELIX 56 56 HIS D 64 TRP D 68 5 5
HELIX 57 57 TRP D 69 LEU D 72 5 4
HELIX 58 58 TYR D 114 PHE D 118 5 5
HELIX 59 59 THR D 122 GLY D 138 1 17
HELIX 60 60 MET D 150 ALA D 159 1 10
HELIX 61 61 PHE D 160 GLY D 162 5 3
HELIX 62 62 SER D 179 ASP D 195 1 17
HELIX 63 63 TYR D 199 GLU D 203 5 5
HELIX 64 64 PRO D 210 TYR D 225 1 16
HELIX 65 65 SER D 227 PHE D 235 1 9
HELIX 66 66 ALA D 273 SER D 288 1 16
HELIX 67 67 ASP D 290 THR D 303 1 14
HELIX 68 68 SER D 313 ALA D 319 1 7
HELIX 69 69 SER D 337 ILE D 348 1 12
HELIX 70 70 ASP D 363 GLU D 368 1 6
HELIX 71 71 GLU D 368 GLN D 382 1 15
HELIX 72 72 ASN E 7 SER E 12 1 6
HELIX 73 73 HIS E 64 TRP E 68 5 5
HELIX 74 74 TRP E 69 LEU E 72 5 4
HELIX 75 75 TYR E 114 PHE E 118 5 5
HELIX 76 76 THR E 122 GLY E 138 1 17
HELIX 77 77 MET E 150 ALA E 159 1 10
HELIX 78 78 PHE E 160 GLY E 162 5 3
HELIX 79 79 SER E 179 ASP E 195 1 17
HELIX 80 80 TYR E 199 GLU E 203 5 5
HELIX 81 81 PRO E 210 TYR E 225 1 16
HELIX 82 82 SER E 227 PHE E 235 1 9
HELIX 83 83 ALA E 273 SER E 288 1 16
HELIX 84 84 ASP E 290 ASP E 302 1 13
HELIX 85 85 SER E 313 ALA E 319 1 7
HELIX 86 86 SER E 337 ILE E 348 1 12
HELIX 87 87 ASP E 363 GLU E 368 1 6
HELIX 88 88 GLU E 368 GLN E 382 1 15
HELIX 89 89 ASN F 7 SER F 12 1 6
HELIX 90 90 HIS F 64 TRP F 68 5 5
HELIX 91 91 TRP F 69 LEU F 72 5 4
HELIX 92 92 TYR F 114 PHE F 118 5 5
HELIX 93 93 THR F 122 GLY F 138 1 17
HELIX 94 94 MET F 150 PHE F 160 1 11
HELIX 95 95 SER F 179 ASP F 195 1 17
HELIX 96 96 TYR F 199 GLU F 203 5 5
HELIX 97 97 PRO F 210 TYR F 225 1 16
HELIX 98 98 SER F 227 PHE F 235 1 9
HELIX 99 99 ALA F 273 SER F 288 1 16
HELIX 100 100 ASP F 290 THR F 303 1 14
HELIX 101 101 SER F 313 MET F 320 1 8
HELIX 102 102 SER F 337 ILE F 348 1 12
HELIX 103 103 ASP F 363 GLU F 368 1 6
HELIX 104 104 GLU F 368 GLN F 382 1 15
HELIX 105 105 ASN G 7 SER G 12 1 6
HELIX 106 106 HIS G 64 TRP G 68 5 5
HELIX 107 107 TRP G 69 LEU G 72 5 4
HELIX 108 108 TYR G 114 PHE G 118 5 5
HELIX 109 109 THR G 122 GLY G 138 1 17
HELIX 110 110 MET G 150 ALA G 159 1 10
HELIX 111 111 PHE G 160 GLY G 162 5 3
HELIX 112 112 SER G 179 ASP G 195 1 17
HELIX 113 113 TYR G 199 GLU G 203 5 5
HELIX 114 114 PRO G 210 TYR G 225 1 16
HELIX 115 115 SER G 227 PHE G 235 1 9
HELIX 116 116 ALA G 273 SER G 288 1 16
HELIX 117 117 ASP G 290 PHE G 301 1 12
HELIX 118 118 ASP G 302 HIS G 304 5 3
HELIX 119 119 SER G 313 ALA G 319 1 7
HELIX 120 120 SER G 337 ILE G 348 1 12
HELIX 121 121 ASP G 363 GLU G 368 1 6
HELIX 122 122 GLU G 368 GLN G 382 1 15
HELIX 123 123 ASN H 7 SER H 12 1 6
HELIX 124 124 HIS H 64 TRP H 68 5 5
HELIX 125 125 TRP H 69 LEU H 72 5 4
HELIX 126 126 TYR H 114 PHE H 118 5 5
HELIX 127 127 THR H 122 GLY H 138 1 17
HELIX 128 128 MET H 150 ALA H 159 1 10
HELIX 129 129 PHE H 160 GLY H 162 5 3
HELIX 130 130 SER H 179 ASP H 195 1 17
HELIX 131 131 TYR H 199 GLU H 203 5 5
HELIX 132 132 PRO H 210 TYR H 225 1 16
HELIX 133 133 SER H 227 PHE H 235 1 9
HELIX 134 134 ALA H 273 SER H 288 1 16
HELIX 135 135 ASP H 290 PHE H 301 1 12
HELIX 136 136 ASP H 302 HIS H 304 5 3
HELIX 137 137 SER H 313 ALA H 319 1 7
HELIX 138 138 SER H 337 ILE H 348 1 12
HELIX 139 139 ASP H 363 GLU H 368 1 6
HELIX 140 140 GLU H 368 GLN H 382 1 15
HELIX 141 141 ASN I 7 SER I 12 1 6
HELIX 142 142 HIS I 64 TRP I 68 5 5
HELIX 143 143 TRP I 69 LEU I 72 5 4
HELIX 144 144 TYR I 114 PHE I 118 5 5
HELIX 145 145 THR I 122 GLY I 138 1 17
HELIX 146 146 MET I 150 ALA I 159 1 10
HELIX 147 147 PHE I 160 GLY I 162 5 3
HELIX 148 148 SER I 179 ASP I 195 1 17
HELIX 149 149 TYR I 199 GLU I 203 5 5
HELIX 150 150 PRO I 210 TYR I 225 1 16
HELIX 151 151 SER I 227 PHE I 235 1 9
HELIX 152 152 ALA I 273 SER I 288 1 16
HELIX 153 153 ASP I 290 PHE I 301 1 12
HELIX 154 154 ASP I 302 HIS I 304 5 3
HELIX 155 155 SER I 313 ALA I 319 1 7
HELIX 156 156 SER I 337 ILE I 348 1 12
HELIX 157 157 ASP I 363 GLU I 368 1 6
HELIX 158 158 GLU I 368 GLN I 382 1 15
HELIX 159 159 ASN J 7 SER J 12 1 6
HELIX 160 160 HIS J 64 TRP J 68 5 5
HELIX 161 161 TRP J 69 LEU J 72 5 4
HELIX 162 162 TYR J 114 PHE J 118 5 5
HELIX 163 163 THR J 122 LEU J 137 1 16
HELIX 164 164 MET J 150 ALA J 159 1 10
HELIX 165 165 PHE J 160 GLY J 162 5 3
HELIX 166 166 SER J 179 ASP J 195 1 17
HELIX 167 167 TYR J 199 GLU J 203 5 5
HELIX 168 168 PRO J 210 TYR J 225 1 16
HELIX 169 169 SER J 227 ARG J 234 1 8
HELIX 170 170 ALA J 273 SER J 288 1 16
HELIX 171 171 ASP J 290 ASP J 302 1 13
HELIX 172 172 SER J 313 ALA J 319 1 7
HELIX 173 173 SER J 337 ILE J 348 1 12
HELIX 174 174 ASP J 363 GLU J 368 1 6
HELIX 175 175 GLU J 368 GLN J 382 1 15
HELIX 176 176 ASN K 7 SER K 12 1 6
HELIX 177 177 HIS K 64 TRP K 68 5 5
HELIX 178 178 TRP K 69 LEU K 72 5 4
HELIX 179 179 TYR K 114 PHE K 118 5 5
HELIX 180 180 THR K 122 GLY K 138 1 17
HELIX 181 181 MET K 150 ALA K 159 1 10
HELIX 182 182 PHE K 160 GLY K 162 5 3
HELIX 183 183 SER K 179 ASP K 195 1 17
HELIX 184 184 TYR K 199 GLU K 203 5 5
HELIX 185 185 PRO K 210 TYR K 225 1 16
HELIX 186 186 SER K 227 ARG K 234 1 8
HELIX 187 187 ALA K 273 SER K 288 1 16
HELIX 188 188 ASP K 290 ASP K 302 1 13
HELIX 189 189 SER K 313 ALA K 319 1 7
HELIX 190 190 SER K 337 ILE K 348 1 12
HELIX 191 191 ASP K 363 GLU K 368 1 6
HELIX 192 192 GLU K 368 ASP K 381 1 14
HELIX 193 193 ASN L 7 SER L 12 1 6
HELIX 194 194 HIS L 64 TRP L 68 5 5
HELIX 195 195 TRP L 69 LEU L 72 5 4
HELIX 196 196 TYR L 114 PHE L 118 5 5
HELIX 197 197 THR L 122 GLY L 138 1 17
HELIX 198 198 MET L 150 ALA L 159 1 10
HELIX 199 199 PHE L 160 GLY L 162 5 3
HELIX 200 200 SER L 179 ASP L 195 1 17
HELIX 201 201 TYR L 199 GLU L 203 5 5
HELIX 202 202 PRO L 210 TYR L 225 1 16
HELIX 203 203 SER L 227 PHE L 235 1 9
HELIX 204 204 ALA L 273 SER L 288 1 16
HELIX 205 205 ASP L 290 PHE L 301 1 12
HELIX 206 206 ASP L 302 HIS L 304 5 3
HELIX 207 207 SER L 313 ALA L 319 1 7
HELIX 208 208 SER L 337 ILE L 348 1 12
HELIX 209 209 ASP L 363 GLU L 368 1 6
HELIX 210 210 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 GLY A 147 1 N ALA A 143 O CYS A 52
SHEET 6 AA 6 ILE A 169 PRO A 171 1 O VAL A 170 N GLY A 147
SHEET 1 AB 3 ALA A 325 CYS A 329 0
SHEET 2 AB 3 SER A 351 VAL A 355 1 O ARG A 352 N ILE A 327
SHEET 3 AB 3 GLN K 382 SER K 383 1 O SER K 383 N VAL A 355
SHEET 1 BA 6 ASP B 17 THR B 25 0
SHEET 2 BA 6 ILE B 31 TRP B 42 -1 O LEU B 32 N PHE B 24
SHEET 3 BA 6 PHE B 85 LEU B 89 -1 O ILE B 86 N TRP B 42
SHEET 4 BA 6 CYS B 52 CYS B 56 1 O VAL B 53 N ILE B 87
SHEET 5 BA 6 ILE B 142 GLY B 147 1 N ALA B 143 O CYS B 52
SHEET 6 BA 6 ILE B 169 PRO B 171 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 GLY C 147 1 N ALA C 143 O CYS C 52
SHEET 6 CA 6 ILE C 169 PRO C 171 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 GLY D 147 1 N ALA D 143 O CYS D 52
SHEET 6 DA 6 ILE D 169 PRO D 171 1 O VAL D 170 N GLY D 147
SHEET 1 DB 2 ALA D 325 ALA D 330 0
SHEET 2 DB 2 SER D 351 VAL D 356 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 GLY E 147 1 N ALA E 143 O CYS E 52
SHEET 6 EA 6 ILE E 169 PRO E 171 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 GLY F 147 1 N ALA F 143 O CYS F 52
SHEET 6 FA 6 ILE F 169 PRO F 171 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 GLY G 147 1 N ALA G 143 O CYS G 52
SHEET 6 GA 6 ILE G 169 PRO G 171 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 GLY H 147 1 N ALA H 143 O CYS H 52
SHEET 6 HA 6 ILE H 169 PRO H 171 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 GLY I 147 1 N ALA I 143 O CYS I 52
SHEET 6 IA 6 ILE I 169 PRO I 171 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 GLY J 147 1 N ALA J 143 O CYS J 52
SHEET 6 JA 6 ILE J 169 PRO J 171 1 O VAL J 170 N GLY J 147
SHEET 1 JB 2 PHE J 235 HIS J 236 0
SHEET 2 JB 2 GLN J 269 PRO J 270 1 O GLN J 269 N HIS J 236
SHEET 1 JC 2 ALA J 325 CYS J 329 0
SHEET 2 JC 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 GLY K 147 1 N ALA K 143 O CYS K 52
SHEET 6 KA 6 ILE K 169 PRO K 171 1 O VAL K 170 N GLY K 147
SHEET 1 KB 2 PHE K 235 HIS K 236 0
SHEET 2 KB 2 GLN K 269 PRO K 270 1 O GLN K 269 N HIS K 236
SHEET 1 KC 2 ALA K 325 CYS K 329 0
SHEET 2 KC 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 GLY L 147 1 N ALA L 143 O CYS L 52
SHEET 6 LA 6 ILE L 169 PRO L 171 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 1.34
LINK C2ABOAS A 149 C3' CSC A1383 1555 1555 1.70
LINK C ALA B 148 N OAS B 149 1555 1555 1.33
LINK C2ABOAS B 149 O1 CSC B1384 1555 1555 1.28
LINK C1ABOAS B 149 O1 CSC B1384 1555 1555 1.66
LINK C OAS B 149 N MET B 150 1555 1555 1.33
LINK C ALA C 148 N OAS C 149 1555 1555 1.32
LINK C2ABOAS C 149 O1 CSC C1383 1555 1555 1.54
LINK C OAS C 149 N MET C 150 1555 1555 1.33
LINK C2ABOAS C 149 C3 CSC C1383 1555 1555 1.79
LINK C ALA D 148 N OAS D 149 1555 1555 1.33
LINK C OAS D 149 N MET D 150 1555 1555 1.33
LINK C2ABOAS D 149 O1 CSC D1383 1555 1555 1.43
LINK C1ABOAS D 149 O1 CSC D1383 1555 1555 1.80
LINK C ALA E 148 N OAS E 149 1555 1555 1.34
LINK OACBOAS E 149 O1 CSC E1383 1555 1555 1.62
LINK C1ABOAS E 149 O1 CSC E1383 1555 1555 1.44
LINK C2ABOAS E 149 O1 CSC E1383 1555 1555 1.21
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 OACBOAS F 149 O1 BCSC F1383 1555 1555 1.72
LINK C1ABOAS F 149 O1 BCSC F1383 1555 1555 1.72
LINK C2ABOAS F 149 O1 BCSC F1383 1555 1555 1.49
LINK C2ABOAS F 149 C3'BCSC F1383 1555 1555 1.31
LINK C OAS F 149 N MET F 150 1555 1555 1.32
LINK C ALA G 148 N OAS G 149 1555 1555 1.33
LINK C2ABOAS G 149 C3 CSC G1383 1555 1555 1.69
LINK C2ABOAS G 149 O1 CSC G1383 1555 1555 1.49
LINK C1ABOAS G 149 O1 CSC G1383 1555 1555 1.39
LINK C2ABOAS G 149 C3' CSC G1383 1555 1555 1.49
LINK OACBOAS G 149 O1 CSC G1383 1555 1555 1.36
LINK C OAS G 149 N MET G 150 1555 1555 1.33
LINK C ALA H 148 N OAS H 149 1555 1555 1.34
LINK OG AOAS H 149 C20ACSC H1383 1555 1555 1.69
LINK CB AOAS H 149 C20ACSC H1383 1555 1555 1.66
LINK C2ABOAS H 149 C3'BCSC H1383 1555 1555 1.43
LINK C2ABOAS H 149 O1 BCSC H1383 1555 1555 1.63
LINK C OAS H 149 N MET H 150 1555 1555 1.34
LINK C ALA I 148 N OAS I 149 1555 1555 1.32
LINK C2ABOAS I 149 O1 CSC I1383 1555 1555 1.38
LINK C1ABOAS I 149 O1 CSC I1383 1555 1555 1.68
LINK OACBOAS I 149 O1 CSC I1383 1555 1555 1.75
LINK C OAS I 149 N MET I 150 1555 1555 1.34
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 1.33
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 OACBOAS L 149 O1 BCSC L1383 1555 1555 1.54
LINK C1ABOAS L 149 O1 BCSC L1383 1555 1555 1.46
LINK C2ABOAS L 149 O1 BCSC L1383 1555 1555 1.34
LINK C2ABOAS L 149 C3'BCSC L1383 1555 1555 1.24
LINK OG AOAS L 149 C20ACSC L1383 1555 1555 1.59
LINK CB AOAS L 149 C20ACSC L1383 1555 1555 1.70
LINK C OAS L 149 N MET L 150 1555 1555 1.33
SITE 1 AC1 9 THR A 58 LEU A 59 THR A 60 ARG A 218
SITE 2 AC1 9 TYR A 225 LYS A 226 ARG A 234 ASP A 363
SITE 3 AC1 9 MET A 367
SITE 1 AC2 12 THR B 58 LEU B 59 THR B 60 ARG B 218
SITE 2 AC2 12 TYR B 225 LYS B 226 ARG B 234 GLN B 281
SITE 3 AC2 12 ASP B 363 MET B 367 HOH B2006 HOH B2051
SITE 1 AC3 10 THR C 58 LEU C 59 THR C 60 ARG C 218
SITE 2 AC3 10 TYR C 225 LYS C 226 ARG C 234 TYR C 277
SITE 3 AC3 10 MET C 367 HOH C2006
SITE 1 AC4 9 THR D 58 LEU D 59 THR D 60 ARG D 218
SITE 2 AC4 9 TYR D 225 LYS D 226 ARG D 234 TYR D 277
SITE 3 AC4 9 MET D 367
SITE 1 AC5 12 THR E 58 LEU E 59 THR E 60 ARG E 218
SITE 2 AC5 12 TYR E 225 LYS E 226 ARG E 234 TYR E 277
SITE 3 AC5 12 GLN E 281 ASP E 363 MET E 367 HOH E2046
SITE 1 AC6 13 THR F 58 LEU F 59 THR F 60 MET F 150
SITE 2 AC6 13 ARG F 218 TYR F 225 LYS F 226 ARG F 234
SITE 3 AC6 13 TYR F 277 PHE F 301 ASP F 363 PHE F 365
SITE 4 AC6 13 MET F 367
SITE 1 AC7 12 THR G 58 LEU G 59 THR G 60 SER G 61
SITE 2 AC7 12 ARG G 218 TYR G 225 LYS G 226 ARG G 234
SITE 3 AC7 12 GLN G 281 ASP G 363 MET G 367 HOH G2052
SITE 1 AC8 11 THR H 58 LEU H 59 THR H 60 SER H 61
SITE 2 AC8 11 MET H 150 ARG H 218 TYR H 225 LYS H 226
SITE 3 AC8 11 ARG H 234 HIS H 362 ASP H 363
SITE 1 AC9 9 THR I 58 LEU I 59 THR I 60 ARG I 218
SITE 2 AC9 9 TYR I 225 LYS I 226 ARG I 234 GLN I 281
SITE 3 AC9 9 ASP I 363
SITE 1 BC1 11 THR J 58 LEU J 59 THR J 60 ARG J 218
SITE 2 BC1 11 TYR J 225 LYS J 226 ARG J 234 TYR J 277
SITE 3 BC1 11 GLN J 281 ASP J 363 PHE J 365
SITE 1 BC2 10 THR K 58 LEU K 59 THR K 60 ARG K 218
SITE 2 BC2 10 TYR K 225 LYS K 226 ARG K 234 TYR K 277
SITE 3 BC2 10 GLN K 281 ASP K 363
SITE 1 BC3 14 THR L 58 LEU L 59 THR L 60 MET L 150
SITE 2 BC3 14 ARG L 218 TYR L 225 LYS L 226 ARG L 234
SITE 3 BC3 14 TYR L 277 GLN L 281 PHE L 301 HIS L 362
SITE 4 BC3 14 ASP L 363 MET L 367
SITE 1 BC4 4 GLU A 157 PHE A 161 THR B 25 ILE B 31
SITE 1 BC5 4 THR A 25 ILE A 31 GLU B 157 PHE B 161
SITE 1 BC6 3 GLU E 157 PHE E 161 THR I 25
SITE 1 BC7 3 THR E 25 ILE E 31 GLU I 157
SITE 1 BC8 2 ARG H 128 GLU H 157
SITE 1 BC9 2 ARG G 128 GLU G 157
SITE 1 CC1 3 ARG D 128 GLU D 157 PHE D 161
SITE 1 CC2 3 ARG F 128 GLU F 157 PHE F 161
SITE 1 CC3 3 ARG C 128 GLU C 157 PHE C 161
SITE 1 CC4 3 ARG L 128 GLU L 157 PHE L 161
SITE 1 CC5 4 SER A 22 ARG B 131 ASP B 135 TYR B 165
SITE 1 CC6 3 ASP A 135 ARG A 140 SER B 22
SITE 1 CC7 4 ARG E 131 ASP E 135 ARG E 140 SER I 22
SITE 1 CC8 2 SER E 22 TYR I 165
SITE 1 CC9 3 ARG I 331 PHE I 338 PHE K 338
CRYST1 122.065 108.865 195.792 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 0.008192 0.000000 0.000004 0.00000
SCALE2 0.000000 0.009186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005107 0.00000
MTRIX1 1 -0.999900 -0.007868 -0.007694 152.90000 1
MTRIX2 1 0.007720 -0.999800 0.019170 20.54000 1
MTRIX3 1 -0.007843 0.019110 0.999800 0.48650 1
MTRIX1 2 -0.793700 0.098220 -0.600400 147.80000 1
MTRIX2 2 0.074380 0.995100 0.064480 1.18500 1
MTRIX3 2 0.603800 0.006523 -0.797100 -19.53000 1
MTRIX1 3 0.793500 -0.098570 -0.600500 58.10000 1
MTRIX2 3 -0.074790 -0.995100 0.064520 -23.72000 1
MTRIX3 3 -0.604000 -0.006288 -0.797000 168.80000 1
MTRIX1 4 1.000000 -0.000317 0.000034 61.05000 1
MTRIX2 4 -0.000317 -1.000000 0.000145 22.01000 1
MTRIX3 4 0.000034 -0.000145 -1.000000 97.90000 1
MTRIX1 5 -0.522700 0.501700 0.689300 110.50000 1
MTRIX2 5 0.337500 0.864200 -0.373100 -7.31200 1
MTRIX3 5 -0.782800 0.037600 -0.621100 56.30000 1
MTRIX1 6 0.533100 0.492500 0.687900 -8.14000 1
MTRIX2 6 0.379900 -0.865900 0.325400 -43.33000 1
MTRIX3 6 0.755900 0.087870 -0.648700 58.61000 1
MTRIX1 7 0.532900 -0.492900 -0.687800 37.52000 1
MTRIX2 7 0.381500 0.865500 -0.324700 -53.93000 1
MTRIX3 7 0.755300 -0.089380 0.649200 -49.04000 1
MTRIX1 8 -0.999900 0.008610 0.007416 213.00000 1
MTRIX2 8 0.008462 0.999800 -0.019740 -0.11630 1
MTRIX3 8 -0.007584 -0.019680 -0.999800 99.23000 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 -0.801100 0.096760 0.590700 156.80000 1
MTRIX2 10 -0.048420 -0.994100 0.097170 -28.94000 1
MTRIX3 10 0.596600 0.049240 0.801000 -68.67000 1
MTRIX1 11 -0.522600 -0.501900 -0.689200 220.90000 1
MTRIX2 11 0.337500 -0.864100 0.373300 -45.41000 1
MTRIX3 11 -0.782900 -0.037530 0.621000 44.09000 1
TER 2744 GLN A 382
TER 5499 SER B 383
TER 8258 GLN C 382
TER 11004 GLN D 382
TER 13728 GLN E 382
TER 16425 GLN F 382
TER 19133 GLN G 382
TER 21848 GLN H 382
TER 24584 SER I 383
TER 27299 LEU J 384
TER 29994 LEU K 384
TER 32686 GLN L 382
MASTER 2453 0 39 210 101 0 53 3933548 12 543 420
END |