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HEADER HYDROLASE 16-JUN-26 27XP
TITLE CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE FROM RHODOCOCCUS
TITLE 2 SP. EG-5 N COMPLEX WITH PARANITROPHENYL BUTYRATE (PNPB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO-ETHYLHEXYLPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. EG-5;
SOURCE 3 ORGANISM_TAXID: 1747801;
SOURCE 4 GENE: MEHPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MONO-BUTYL PHTHALATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
REVDAT 1 01-JUL-26 27XP 0
JRNL AUTH S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
JRNL TITL CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE FROM
JRNL TITL 2 RHODOCOCCUS SP. EG-5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 101747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 5006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7058
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE SET COUNT : 375
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22175
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.57500
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 4.97400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.274
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.284
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.363
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.797
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.761
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22675 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 21471 ; 0.000 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30806 ; 1.383 ; 1.811
REMARK 3 BOND ANGLES OTHERS (DEGREES): 49371 ; 0.456 ; 1.748
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2881 ; 5.776 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 153 ; 9.160 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3593 ;14.414 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3459 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26930 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5118 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4296 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 387 ; 0.247 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11102 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 247 ; 0.147 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 11584 ; 0.686 ; 1.721
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11584 ; 0.685 ; 1.721
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14445 ; 1.034 ; 3.092
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14446 ; 1.034 ; 3.092
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11091 ; 0.655 ; 1.750
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11092 ; 0.655 ; 1.750
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 16361 ; 0.993 ; 3.214
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 16362 ; 0.993 ; 3.214
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 45
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 297 NULL
REMARK 3 1 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 2 A 3 A 298 NULL
REMARK 3 2 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 A 5 A 298 NULL
REMARK 3 3 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 4 A 3 A 297 NULL
REMARK 3 4 A 3 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 A 5 A 297 NULL
REMARK 3 5 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 6 A 3 A 298 NULL
REMARK 3 6 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 7 A 4 A 297 NULL
REMARK 3 7 A 4 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 8 A 5 A 298 NULL
REMARK 3 8 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 9 A 3 A 297 NULL
REMARK 3 9 A 3 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 10 A 5 A 298 NULL
REMARK 3 10 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 11
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 11 A 5 A 298 NULL
REMARK 3 11 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 12 A 5 A 297 NULL
REMARK 3 12 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 13
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 13 A 5 A 298 NULL
REMARK 3 13 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 14
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 14 A 5 A 298 NULL
REMARK 3 14 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 15
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 15 A 5 A 298 NULL
REMARK 3 15 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 16
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 16 A 5 A 298 NULL
REMARK 3 16 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 17
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 17
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 17 A 5 A 297 NULL
REMARK 3 17 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 18
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 18
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 18 A 5 A 298 NULL
REMARK 3 18 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 19
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 19
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 19 A 3 A 298 NULL
REMARK 3 19 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 20
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 20
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 20 A 5 A 298 NULL
REMARK 3 20 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 21
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 21
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 21 A 3 A 298 NULL
REMARK 3 21 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 22
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 22
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 22 A 4 A 298 NULL
REMARK 3 22 A 4 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 23
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 23
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 23 A 5 A 298 NULL
REMARK 3 23 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 24
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 24
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 24 A 3 A 298 NULL
REMARK 3 24 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 25
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 25
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 25 A 5 A 298 NULL
REMARK 3 25 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 26
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 26
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 26 A 5 A 298 NULL
REMARK 3 26 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 27
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 27
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 27 A 5 A 298 NULL
REMARK 3 27 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 28
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 28
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 28 A 5 A 298 NULL
REMARK 3 28 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 29
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 29
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 29 A 5 A 298 NULL
REMARK 3 29 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 30
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 30
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 30 A 5 A 298 NULL
REMARK 3 30 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 31
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 31
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 31 A 5 A 297 NULL
REMARK 3 31 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 32
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 32
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 32 A 3 A 298 NULL
REMARK 3 32 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 33
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 33
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 33 A 4 A 298 NULL
REMARK 3 33 A 4 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 34
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 34
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 34 A 5 A 298 NULL
REMARK 3 34 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 35
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 35
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 35 A 3 A 298 NULL
REMARK 3 35 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 36
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 36
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 36 A 5 A 298 NULL
REMARK 3 36 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 37
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 37
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 37 A 5 A 298 NULL
REMARK 3 37 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 38
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 38
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 38 A 5 A 298 NULL
REMARK 3 38 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 39
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 39
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 39 A 5 A 297 NULL
REMARK 3 39 A 5 A 297 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 40
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 40
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 40 A 4 A 298 NULL
REMARK 3 40 A 4 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 41
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 41
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 41 A 5 A 298 NULL
REMARK 3 41 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 42
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 42
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 42 A 3 A 298 NULL
REMARK 3 42 A 3 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 43
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 43
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 43 A 5 A 298 NULL
REMARK 3 43 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 44
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 44
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 44 A 4 A 298 NULL
REMARK 3 44 A 4 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 45
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 45
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 45 A 5 A 298 NULL
REMARK 3 45 A 5 A 298 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 298
REMARK 3 ORIGIN FOR THE GROUP (A):-111.3221 -53.3913 101.0916
REMARK 3 T TENSOR
REMARK 3 T11: 0.0479 T22: 0.1470
REMARK 3 T33: 0.1417 T12: 0.0034
REMARK 3 T13: -0.0192 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.7884 L22: 0.0545
REMARK 3 L33: 2.4741 L12: -0.1780
REMARK 3 L13: -0.3469 L23: 0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: -0.0552 S13: -0.1499
REMARK 3 S21: 0.0249 S22: -0.0103 S23: 0.0158
REMARK 3 S31: 0.1153 S32: 0.1389 S33: 0.0476
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -98.2771 -53.5064 62.2588
REMARK 3 T TENSOR
REMARK 3 T11: 0.0071 T22: 0.1878
REMARK 3 T33: 0.1027 T12: -0.0046
REMARK 3 T13: -0.0064 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.5632 L22: 0.6165
REMARK 3 L33: 1.8172 L12: 0.0644
REMARK 3 L13: -0.2100 L23: 0.3097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.1324 S13: -0.0013
REMARK 3 S21: -0.0613 S22: 0.0258 S23: -0.0268
REMARK 3 S31: -0.0167 S32: 0.0890 S33: -0.0097
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -74.5844 -56.2901 24.1667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0146 T22: 0.1785
REMARK 3 T33: 0.0994 T12: 0.0044
REMARK 3 T13: -0.0115 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.1238 L22: 0.0482
REMARK 3 L33: 2.1304 L12: 0.2213
REMARK 3 L13: -0.3397 L23: 0.0160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.0761 S13: -0.0826
REMARK 3 S21: 0.0095 S22: -0.0358 S23: -0.0137
REMARK 3 S31: 0.1564 S32: -0.0075 S33: 0.0223
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -63.4515 -49.9414 -14.7463
REMARK 3 T TENSOR
REMARK 3 T11: 0.0158 T22: 0.1088
REMARK 3 T33: 0.0928 T12: 0.0120
REMARK 3 T13: -0.0097 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.5858 L22: 0.5168
REMARK 3 L33: 2.0431 L12: 0.0821
REMARK 3 L13: -0.4124 L23: 0.0777
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.1197 S13: 0.0084
REMARK 3 S21: -0.0725 S22: 0.0278 S23: 0.0388
REMARK 3 S31: -0.1105 S32: -0.2295 S33: -0.0450
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A):-134.4433 -38.8097 52.8333
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.0556
REMARK 3 T33: 0.1330 T12: 0.0291
REMARK 3 T13: -0.0209 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.2297 L22: 0.9376
REMARK 3 L33: 2.4087 L12: -0.4580
REMARK 3 L13: -0.3287 L23: 0.5554
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.0458 S13: -0.0697
REMARK 3 S21: -0.0347 S22: -0.0690 S23: 0.1509
REMARK 3 S31: -0.1295 S32: -0.1768 S33: 0.0600
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0069 -38.7213 52.9373
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.0328
REMARK 3 T33: 0.0994 T12: -0.0040
REMARK 3 T13: -0.0032 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.8359 L22: 0.4333
REMARK 3 L33: 1.7798 L12: 0.0790
REMARK 3 L13: -0.1386 L23: -0.4586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.1142 S13: 0.0325
REMARK 3 S21: 0.1100 S22: -0.0276 S23: 0.0240
REMARK 3 S31: -0.1214 S32: -0.0805 S33: 0.0343
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -35.9175 -30.6435 14.1929
REMARK 3 T TENSOR
REMARK 3 T11: 0.1869 T22: 0.0178
REMARK 3 T33: 0.1094 T12: -0.0222
REMARK 3 T13: -0.0012 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.2101 L22: 0.8154
REMARK 3 L33: 1.8690 L12: 0.4088
REMARK 3 L13: -0.0766 L23: -0.3249
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: -0.0024 S13: -0.0502
REMARK 3 S21: -0.1086 S22: -0.0133 S23: -0.0898
REMARK 3 S31: 0.0182 S32: 0.0944 S33: 0.0587
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A):-139.9338 -26.6917 91.6242
REMARK 3 T TENSOR
REMARK 3 T11: 0.1908 T22: 0.0239
REMARK 3 T33: 0.0922 T12: 0.0373
REMARK 3 T13: -0.0216 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.5756 L22: 0.9258
REMARK 3 L33: 2.4234 L12: 0.2268
REMARK 3 L13: -0.4739 L23: 0.1988
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: -0.0880 S13: 0.0530
REMARK 3 S21: 0.1166 S22: -0.0178 S23: -0.0182
REMARK 3 S31: -0.1793 S32: 0.0579 S33: -0.0193
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0576 -7.4405 -23.7155
REMARK 3 T TENSOR
REMARK 3 T11: 0.3124 T22: 0.0268
REMARK 3 T33: 0.1071 T12: -0.0446
REMARK 3 T13: 0.0071 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.9601 L22: 0.6510
REMARK 3 L33: 1.7676 L12: -0.1633
REMARK 3 L13: 0.2899 L23: -0.1187
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: -0.1314 S13: -0.0025
REMARK 3 S21: 0.0478 S22: -0.0067 S23: 0.0333
REMARK 3 S31: 0.0916 S32: -0.0054 S33: -0.0109
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6876 5.3230 -62.4189
REMARK 3 T TENSOR
REMARK 3 T11: 0.2491 T22: 0.0329
REMARK 3 T33: 0.1670 T12: -0.0004
REMARK 3 T13: 0.0159 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0611 L22: 1.4064
REMARK 3 L33: 3.0233 L12: -0.2437
REMARK 3 L13: 0.2686 L23: -0.2677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: 0.0388 S13: 0.0304
REMARK 3 S21: -0.1187 S22: -0.0981 S23: -0.2514
REMARK 3 S31: 0.1522 S32: 0.2803 S33: 0.0760
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 27XP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-26.
REMARK 100 THE DEPOSITION ID IS D_1300075706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-25
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101792
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 24.292
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM MALONATE PH 7.4 20% PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 122.44500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 122.44500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 122.44500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 122.44500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, 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 1
REMARK 465 LYS A 142
REMARK 465 PHE A 143
REMARK 465 ARG A 144
REMARK 465 ASP A 145
REMARK 465 VAL A 146
REMARK 465 TYR A 299
REMARK 465 ALA A 300
REMARK 465 THR A 301
REMARK 465 ARG A 302
REMARK 465 ARG A 303
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 ASP B 140
REMARK 465 ALA B 141
REMARK 465 LYS B 142
REMARK 465 PHE B 143
REMARK 465 ARG B 144
REMARK 465 TYR B 299
REMARK 465 ALA B 300
REMARK 465 THR B 301
REMARK 465 ARG B 302
REMARK 465 ARG B 303
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 THR C 139
REMARK 465 ASP C 140
REMARK 465 ALA C 141
REMARK 465 LYS C 142
REMARK 465 PHE C 143
REMARK 465 ARG C 144
REMARK 465 ASP C 145
REMARK 465 TYR C 299
REMARK 465 ALA C 300
REMARK 465 THR C 301
REMARK 465 ARG C 302
REMARK 465 ARG C 303
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 ASP D 4
REMARK 465 ALA D 141
REMARK 465 LYS D 142
REMARK 465 TYR D 299
REMARK 465 ALA D 300
REMARK 465 THR D 301
REMARK 465 ARG D 302
REMARK 465 ARG D 303
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 141
REMARK 465 LYS E 142
REMARK 465 PHE E 143
REMARK 465 ARG E 144
REMARK 465 ASP E 145
REMARK 465 TYR E 299
REMARK 465 ALA E 300
REMARK 465 THR E 301
REMARK 465 ARG E 302
REMARK 465 ARG E 303
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 THR F 3
REMARK 465 ASP F 4
REMARK 465 THR F 139
REMARK 465 ASP F 140
REMARK 465 ALA F 141
REMARK 465 LYS F 142
REMARK 465 PHE F 143
REMARK 465 TYR F 299
REMARK 465 ALA F 300
REMARK 465 THR F 301
REMARK 465 ARG F 302
REMARK 465 ARG F 303
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 PHE G 143
REMARK 465 ARG G 144
REMARK 465 ASP G 145
REMARK 465 VAL G 146
REMARK 465 GLU G 147
REMARK 465 PHE G 148
REMARK 465 TYR G 149
REMARK 465 ASP G 150
REMARK 465 ALA G 151
REMARK 465 ILE G 152
REMARK 465 THR G 153
REMARK 465 ARG G 154
REMARK 465 TYR G 299
REMARK 465 ALA G 300
REMARK 465 THR G 301
REMARK 465 ARG G 302
REMARK 465 ARG G 303
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 THR H 3
REMARK 465 ALA H 141
REMARK 465 LYS H 142
REMARK 465 PHE H 143
REMARK 465 ARG H 144
REMARK 465 TYR H 299
REMARK 465 ALA H 300
REMARK 465 THR H 301
REMARK 465 ARG H 302
REMARK 465 ARG H 303
REMARK 465 MET I 1
REMARK 465 ASN I 2
REMARK 465 THR I 3
REMARK 465 ASP I 4
REMARK 465 LYS I 142
REMARK 465 TYR I 299
REMARK 465 ALA I 300
REMARK 465 THR I 301
REMARK 465 ARG I 302
REMARK 465 ARG I 303
REMARK 465 MET J 1
REMARK 465 ASN J 2
REMARK 465 LYS J 142
REMARK 465 PHE J 143
REMARK 465 ARG J 144
REMARK 465 ASP J 145
REMARK 465 VAL J 146
REMARK 465 TYR J 299
REMARK 465 ALA J 300
REMARK 465 THR J 301
REMARK 465 ARG J 302
REMARK 465 ARG J 303
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 HD1 HIS D 35 HE ARG D 109 1.28
REMARK 500 HE1 TYR G 254 HG23 THR G 264 1.28
REMARK 500 HD1 HIS F 35 HE ARG F 109 1.29
REMARK 500 HE1 TYR A 254 HG23 THR A 264 1.31
REMARK 500 HD1 HIS H 35 HE ARG H 109 1.32
REMARK 500 HD1 HIS A 35 HE ARG A 109 1.32
REMARK 500 HD1 HIS B 35 HE ARG B 109 1.32
REMARK 500 HD1 HIS E 35 HE ARG E 109 1.33
REMARK 500 HD1 HIS I 35 HE ARG I 109 1.34
REMARK 500 HG SER E 6 O ASP E 21 1.35
REMARK 500 OE2 GLU B 193 HZ3 LYS C 88 1.59
REMARK 500 OG SER E 6 O ASP E 21 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 MET B 102 CG - SD - CE ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG B 295 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLU C 282 CG - CD - OE2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ARG C 295 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 MET E 102 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 MET E 204 CG - SD - CE ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG E 224 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG E 295 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG G 171 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET G 204 CG - SD - CE ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG G 295 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG H 295 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG J 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET J 102 CG - SD - CE ANGL. DEV. = -11.4 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
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 LEU A 5 -101.50 -36.17
REMARK 500 SER A 6 57.72 -94.58
REMARK 500 SER A 108 -121.41 58.28
REMARK 500 TYR A 209 -50.91 -124.25
REMARK 500 ASN A 231 41.22 -107.87
REMARK 500 SER B 108 -123.89 61.70
REMARK 500 TYR B 209 -50.61 -127.11
REMARK 500 ASN B 275 66.68 -101.00
REMARK 500 ASP C 4 -127.06 88.13
REMARK 500 LEU C 5 73.29 102.37
REMARK 500 SER C 108 -122.58 60.91
REMARK 500 TYR C 209 -51.91 -123.70
REMARK 500 ASN C 231 40.35 -105.09
REMARK 500 SER D 6 47.59 -88.24
REMARK 500 SER D 108 -122.87 60.04
REMARK 500 TYR D 209 -50.63 -126.16
REMARK 500 ASN D 275 68.74 -100.39
REMARK 500 ASP E 4 -133.24 175.27
REMARK 500 LEU E 5 72.39 104.58
REMARK 500 SER E 108 -122.90 60.04
REMARK 500 TYR E 209 -52.76 -123.71
REMARK 500 SER F 108 -123.87 60.47
REMARK 500 ASP F 145 -64.18 78.55
REMARK 500 TYR F 209 -53.14 -121.99
REMARK 500 SER G 108 -122.28 60.82
REMARK 500 ALA G 141 0.28 -65.27
REMARK 500 TYR G 209 -51.58 -124.22
REMARK 500 ASN G 231 41.82 -105.54
REMARK 500 LEU H 5 78.35 -169.43
REMARK 500 SER H 6 47.57 -85.36
REMARK 500 SER H 108 -123.77 60.62
REMARK 500 ALA H 158 -1.37 72.26
REMARK 500 TYR H 209 -51.11 -124.34
REMARK 500 ASN H 231 41.44 -106.51
REMARK 500 ASN H 275 67.84 -100.44
REMARK 500 VAL I 7 123.65 26.38
REMARK 500 SER I 108 -123.28 61.28
REMARK 500 ALA I 158 -4.16 68.62
REMARK 500 TYR I 209 -51.07 -123.80
REMARK 500 ASN I 275 68.75 -100.36
REMARK 500 ALA I 297 64.33 66.85
REMARK 500 SER J 6 27.48 80.46
REMARK 500 SER J 108 -122.66 61.26
REMARK 500 TYR J 209 -51.12 -124.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 224 0.14 SIDE CHAIN
REMARK 500 ARG B 286 0.08 SIDE CHAIN
REMARK 500 ARG C 16 0.12 SIDE CHAIN
REMARK 500 ARG C 224 0.12 SIDE CHAIN
REMARK 500 ARG E 154 0.09 SIDE CHAIN
REMARK 500 ARG F 224 0.08 SIDE CHAIN
REMARK 500 ARG G 91 0.10 SIDE CHAIN
REMARK 500 ARG G 109 0.07 SIDE CHAIN
REMARK 500 ARG G 224 0.10 SIDE CHAIN
REMARK 500 ARG G 243 0.10 SIDE CHAIN
REMARK 500 ARG I 91 0.08 SIDE CHAIN
REMARK 500 ARG J 18 0.08 SIDE CHAIN
REMARK 500 ARG J 224 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 27XP A 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP A A0A0U5ADH4 1 303
DBREF1 27XP B 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP B A0A0U5ADH4 1 303
DBREF1 27XP C 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP C A0A0U5ADH4 1 303
DBREF1 27XP D 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP D A0A0U5ADH4 1 303
DBREF1 27XP E 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP E A0A0U5ADH4 1 303
DBREF1 27XP F 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP F A0A0U5ADH4 1 303
DBREF1 27XP G 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP G A0A0U5ADH4 1 303
DBREF1 27XP H 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP H A0A0U5ADH4 1 303
DBREF1 27XP I 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP I A0A0U5ADH4 1 303
DBREF1 27XP J 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 27XP J A0A0U5ADH4 1 303
SEQRES 1 A 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 A 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 A 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 A 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 A 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 A 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 A 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 A 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 A 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 A 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 A 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 A 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 A 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 A 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 A 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 A 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 A 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 A 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 A 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 A 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 A 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 A 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 A 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 A 303 ALA THR ARG ARG
SEQRES 1 B 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 B 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 B 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 B 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 B 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 B 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 B 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 B 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 B 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 B 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 B 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 B 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 B 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 B 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 B 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 B 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 B 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 B 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 B 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 B 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 B 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 B 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 B 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 B 303 ALA THR ARG ARG
SEQRES 1 C 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 C 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 C 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 C 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 C 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 C 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 C 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 C 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 C 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 C 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 C 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 C 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 C 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 C 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 C 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 C 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 C 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 C 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 C 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 C 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 C 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 C 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 C 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 C 303 ALA THR ARG ARG
SEQRES 1 D 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 D 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 D 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 D 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 D 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 D 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 D 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 D 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 D 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 D 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 D 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 D 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 D 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 D 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 D 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 D 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 D 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 D 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 D 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 D 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 D 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 D 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 D 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 D 303 ALA THR ARG ARG
SEQRES 1 E 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 E 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 E 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 E 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 E 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 E 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 E 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 E 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 E 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 E 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 E 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 E 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 E 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 E 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 E 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 E 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 E 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 E 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 E 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 E 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 E 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 E 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 E 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 E 303 ALA THR ARG ARG
SEQRES 1 F 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 F 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 F 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 F 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 F 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 F 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 F 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 F 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 F 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 F 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 F 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 F 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 F 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 F 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 F 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 F 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 F 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 F 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 F 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 F 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 F 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 F 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 F 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 F 303 ALA THR ARG ARG
SEQRES 1 G 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 G 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 G 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 G 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 G 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 G 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 G 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 G 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 G 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 G 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 G 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 G 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 G 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 G 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 G 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 G 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 G 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 G 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 G 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 G 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 G 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 G 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 G 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 G 303 ALA THR ARG ARG
SEQRES 1 H 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 H 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 H 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 H 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 H 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 H 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 H 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 H 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 H 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 H 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 H 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 H 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 H 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 H 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 H 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 H 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 H 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 H 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 H 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 H 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 H 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 H 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 H 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 H 303 ALA THR ARG ARG
SEQRES 1 I 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 I 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 I 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 I 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 I 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 I 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 I 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 I 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 I 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 I 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 I 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 I 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 I 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 I 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 I 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 I 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 I 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 I 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 I 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 I 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 I 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 I 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 I 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 I 303 ALA THR ARG ARG
SEQRES 1 J 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 J 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 J 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 J 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 J 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 J 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 J 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 J 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 J 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 J 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 J 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 J 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 J 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 J 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 J 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 J 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 J 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 J 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 J 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 J 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 J 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 J 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 J 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 J 303 ALA THR ARG ARG
HET NPO F 401 15
HETNAM NPO P-NITROPHENOL
FORMUL 11 NPO C6 H5 N O3
FORMUL 12 HOH *4(H2 O)
HELIX 1 AA1 GLY A 43 GLY A 46 5 4
HELIX 2 AA2 TRP A 47 LYS A 57 1 11
HELIX 3 AA3 THR A 77 TRP A 81 5 5
HELIX 4 AA4 THR A 82 GLY A 98 1 17
HELIX 5 AA5 ARG A 109 MET A 121 1 13
HELIX 6 AA6 SER A 133 GLY A 138 1 6
HELIX 7 AA7 PHE A 148 SER A 155 1 8
HELIX 8 AA8 SER A 161 TYR A 174 1 14
HELIX 9 AA9 PRO A 179 VAL A 191 1 13
HELIX 10 AB1 LYS A 192 GLU A 206 1 15
HELIX 11 AB2 TYR A 209 PHE A 226 1 18
HELIX 12 AB3 PRO A 246 LEU A 259 1 14
HELIX 13 AB4 ASN A 275 ARG A 280 1 6
HELIX 14 AB5 ARG A 280 SER A 298 1 19
HELIX 15 AB6 GLY B 43 GLY B 46 5 4
HELIX 16 AB7 TRP B 47 LYS B 57 1 11
HELIX 17 AB8 THR B 77 TRP B 81 5 5
HELIX 18 AB9 THR B 82 GLY B 98 1 17
HELIX 19 AC1 ARG B 109 MET B 121 1 13
HELIX 20 AC2 SER B 133 GLY B 138 1 6
HELIX 21 AC3 VAL B 146 SER B 155 1 10
HELIX 22 AC4 SER B 161 TYR B 174 1 14
HELIX 23 AC5 PRO B 179 VAL B 191 1 13
HELIX 24 AC6 LYS B 192 LYS B 207 1 16
HELIX 25 AC7 TYR B 209 PHE B 226 1 18
HELIX 26 AC8 PRO B 246 LEU B 259 1 14
HELIX 27 AC9 ASN B 275 ARG B 280 1 6
HELIX 28 AD1 ARG B 280 SER B 298 1 19
HELIX 29 AD2 GLY C 43 GLY C 46 5 4
HELIX 30 AD3 TRP C 47 LYS C 57 1 11
HELIX 31 AD4 THR C 77 TRP C 81 5 5
HELIX 32 AD5 THR C 82 GLY C 98 1 17
HELIX 33 AD6 ARG C 109 MET C 121 1 13
HELIX 34 AD7 SER C 133 GLY C 138 1 6
HELIX 35 AD8 GLU C 147 SER C 155 1 9
HELIX 36 AD9 SER C 161 TYR C 174 1 14
HELIX 37 AE1 PRO C 179 VAL C 191 1 13
HELIX 38 AE2 LYS C 192 GLU C 206 1 15
HELIX 39 AE3 TYR C 209 PHE C 226 1 18
HELIX 40 AE4 PRO C 246 LEU C 259 1 14
HELIX 41 AE5 ASN C 275 ARG C 280 1 6
HELIX 42 AE6 ARG C 280 ALA C 297 1 18
HELIX 43 AE7 GLY D 43 GLY D 46 5 4
HELIX 44 AE8 TRP D 47 LYS D 57 1 11
HELIX 45 AE9 THR D 77 TRP D 81 5 5
HELIX 46 AF1 THR D 82 GLY D 98 1 17
HELIX 47 AF2 ARG D 109 MET D 121 1 13
HELIX 48 AF3 SER D 133 GLY D 138 1 6
HELIX 49 AF4 VAL D 146 SER D 155 1 10
HELIX 50 AF5 SER D 161 TYR D 174 1 14
HELIX 51 AF6 PRO D 179 VAL D 191 1 13
HELIX 52 AF7 LYS D 192 LYS D 207 1 16
HELIX 53 AF8 TYR D 209 ALA D 227 1 19
HELIX 54 AF9 PRO D 246 LEU D 259 1 14
HELIX 55 AG1 ASN D 275 ARG D 280 1 6
HELIX 56 AG2 ARG D 280 SER D 298 1 19
HELIX 57 AG3 GLY E 43 GLY E 46 5 4
HELIX 58 AG4 TRP E 47 LYS E 57 1 11
HELIX 59 AG5 THR E 77 TRP E 81 5 5
HELIX 60 AG6 THR E 82 GLY E 98 1 17
HELIX 61 AG7 ARG E 109 MET E 121 1 13
HELIX 62 AG8 SER E 133 GLY E 138 1 6
HELIX 63 AG9 GLU E 147 SER E 155 1 9
HELIX 64 AH1 SER E 161 TYR E 174 1 14
HELIX 65 AH2 PRO E 179 VAL E 191 1 13
HELIX 66 AH3 LYS E 192 GLU E 206 1 15
HELIX 67 AH4 TYR E 209 PHE E 226 1 18
HELIX 68 AH5 PRO E 246 LEU E 259 1 14
HELIX 69 AH6 ASN E 275 ARG E 280 1 6
HELIX 70 AH7 ARG E 280 SER E 298 1 19
HELIX 71 AH8 GLY F 43 GLY F 46 5 4
HELIX 72 AH9 TRP F 47 LYS F 57 1 11
HELIX 73 AI1 THR F 77 TRP F 81 5 5
HELIX 74 AI2 THR F 82 GLY F 98 1 17
HELIX 75 AI3 ARG F 109 MET F 121 1 13
HELIX 76 AI4 VAL F 146 SER F 155 1 10
HELIX 77 AI5 SER F 161 TYR F 174 1 14
HELIX 78 AI6 PRO F 179 VAL F 191 1 13
HELIX 79 AI7 LYS F 192 GLU F 206 1 15
HELIX 80 AI8 TYR F 209 PHE F 226 1 18
HELIX 81 AI9 PRO F 246 LEU F 259 1 14
HELIX 82 AJ1 ASN F 275 ARG F 280 1 6
HELIX 83 AJ2 ARG F 280 SER F 298 1 19
HELIX 84 AJ3 GLY G 43 GLY G 46 5 4
HELIX 85 AJ4 TRP G 47 LYS G 57 1 11
HELIX 86 AJ5 THR G 77 TRP G 81 5 5
HELIX 87 AJ6 THR G 82 GLY G 98 1 17
HELIX 88 AJ7 ARG G 109 MET G 121 1 13
HELIX 89 AJ8 SER G 133 GLY G 138 1 6
HELIX 90 AJ9 SER G 161 TYR G 174 1 14
HELIX 91 AK1 PRO G 179 VAL G 191 1 13
HELIX 92 AK2 LYS G 192 GLU G 206 1 15
HELIX 93 AK3 TYR G 209 PHE G 226 1 18
HELIX 94 AK4 PRO G 246 LEU G 259 1 14
HELIX 95 AK5 ASN G 275 ARG G 280 1 6
HELIX 96 AK6 ARG G 280 SER G 298 1 19
HELIX 97 AK7 GLY H 43 GLY H 46 5 4
HELIX 98 AK8 TRP H 47 LYS H 57 1 11
HELIX 99 AK9 THR H 77 TRP H 81 5 5
HELIX 100 AL1 THR H 82 GLY H 98 1 17
HELIX 101 AL2 ARG H 109 MET H 121 1 13
HELIX 102 AL3 SER H 133 GLY H 138 1 6
HELIX 103 AL4 VAL H 146 SER H 155 1 10
HELIX 104 AL5 SER H 161 TYR H 174 1 14
HELIX 105 AL6 PRO H 179 VAL H 191 1 13
HELIX 106 AL7 LYS H 192 LYS H 207 1 16
HELIX 107 AL8 TYR H 209 PHE H 226 1 18
HELIX 108 AL9 PRO H 246 LEU H 259 1 14
HELIX 109 AM1 ASN H 275 ARG H 280 1 6
HELIX 110 AM2 ARG H 280 SER H 298 1 19
HELIX 111 AM3 GLY I 43 GLY I 46 5 4
HELIX 112 AM4 TRP I 47 LYS I 57 1 11
HELIX 113 AM5 THR I 77 TRP I 81 5 5
HELIX 114 AM6 THR I 82 GLY I 98 1 17
HELIX 115 AM7 ARG I 109 MET I 121 1 13
HELIX 116 AM8 SER I 133 GLY I 138 1 6
HELIX 117 AM9 VAL I 146 SER I 155 1 10
HELIX 118 AN1 SER I 161 TYR I 174 1 14
HELIX 119 AN2 PRO I 179 VAL I 191 1 13
HELIX 120 AN3 LYS I 192 GLU I 206 1 15
HELIX 121 AN4 TYR I 209 PHE I 226 1 18
HELIX 122 AN5 PRO I 246 LEU I 259 1 14
HELIX 123 AN6 ASN I 275 ARG I 280 1 6
HELIX 124 AN7 ARG I 280 ALA I 297 1 18
HELIX 125 AN8 GLY J 43 GLY J 46 5 4
HELIX 126 AN9 TRP J 47 LYS J 57 1 11
HELIX 127 AO1 THR J 77 TRP J 81 5 5
HELIX 128 AO2 THR J 82 GLY J 98 1 17
HELIX 129 AO3 ARG J 109 MET J 121 1 13
HELIX 130 AO4 SER J 133 GLY J 138 1 6
HELIX 131 AO5 PHE J 148 SER J 155 1 8
HELIX 132 AO6 SER J 161 TYR J 174 1 14
HELIX 133 AO7 PRO J 179 VAL J 191 1 13
HELIX 134 AO8 LYS J 192 GLU J 206 1 15
HELIX 135 AO9 TYR J 209 PHE J 226 1 18
HELIX 136 AP1 PRO J 246 LEU J 259 1 14
HELIX 137 AP2 ASN J 275 ARG J 280 1 6
HELIX 138 AP3 ARG J 280 SER J 298 1 19
SHEET 1 AA116 VAL A 7 VAL A 12 0
SHEET 2 AA116 ILE A 15 GLN A 22 -1 O THR A 17 N ILE A 10
SHEET 3 AA116 ARG A 60 PHE A 64 -1 O THR A 63 N ILE A 20
SHEET 4 AA116 VAL A 27 ILE A 31 1 N ILE A 28 O ARG A 60
SHEET 5 AA116 MET A 102 HIS A 107 1 O VAL A 105 N ILE A 31
SHEET 6 AA116 THR A 125 VAL A 131 1 O GLY A 127 N LEU A 104
SHEET 7 AA116 VAL A 234 GLY A 239 1 O VAL A 237 N ILE A 130
SHEET 8 AA116 THR A 263 LEU A 269 1 O LEU A 269 N TRP A 238
SHEET 9 AA116 THR B 263 LEU B 269 -1 O ILE B 268 N THR A 264
SHEET 10 AA116 VAL B 234 GLY B 239 1 N VAL B 236 O HIS B 267
SHEET 11 AA116 THR B 125 VAL B 131 1 N ILE B 130 O VAL B 237
SHEET 12 AA116 MET B 102 HIS B 107 1 N LEU B 104 O GLY B 127
SHEET 13 AA116 VAL B 27 ILE B 31 1 N ILE B 31 O VAL B 105
SHEET 14 AA116 ARG B 60 PHE B 64 1 O ARG B 60 N ILE B 28
SHEET 15 AA116 ILE B 15 GLN B 22 -1 N ILE B 20 O THR B 63
SHEET 16 AA116 VAL B 7 VAL B 12 -1 N ILE B 10 O THR B 17
SHEET 1 AA216 VAL C 7 VAL C 12 0
SHEET 2 AA216 ILE C 15 GLN C 22 -1 O THR C 17 N ILE C 10
SHEET 3 AA216 ARG C 60 PHE C 64 -1 O THR C 63 N ILE C 20
SHEET 4 AA216 VAL C 27 ILE C 31 1 N ILE C 28 O ARG C 60
SHEET 5 AA216 MET C 102 HIS C 107 1 O VAL C 105 N ILE C 31
SHEET 6 AA216 THR C 125 VAL C 131 1 O GLY C 127 N LEU C 104
SHEET 7 AA216 VAL C 234 GLY C 239 1 O VAL C 237 N ILE C 130
SHEET 8 AA216 THR C 263 LEU C 269 1 O HIS C 267 N VAL C 236
SHEET 9 AA216 THR D 263 LEU D 269 -1 O ILE D 268 N THR C 264
SHEET 10 AA216 VAL D 234 GLY D 239 1 N VAL D 236 O HIS D 267
SHEET 11 AA216 THR D 125 VAL D 131 1 N ILE D 130 O VAL D 237
SHEET 12 AA216 MET D 102 HIS D 107 1 N LEU D 104 O GLY D 127
SHEET 13 AA216 VAL D 27 ILE D 31 1 N ILE D 31 O VAL D 105
SHEET 14 AA216 ARG D 60 PHE D 64 1 O ARG D 60 N ILE D 28
SHEET 15 AA216 ILE D 15 GLN D 22 -1 N ILE D 20 O THR D 63
SHEET 16 AA216 VAL D 7 VAL D 12 -1 N ILE D 10 O THR D 17
SHEET 1 AA316 VAL E 7 VAL E 12 0
SHEET 2 AA316 ILE E 15 GLN E 22 -1 O THR E 17 N ILE E 10
SHEET 3 AA316 ARG E 60 PHE E 64 -1 O THR E 63 N ILE E 20
SHEET 4 AA316 VAL E 27 ILE E 31 1 N ILE E 28 O ARG E 60
SHEET 5 AA316 MET E 102 HIS E 107 1 O VAL E 105 N ILE E 31
SHEET 6 AA316 THR E 125 VAL E 131 1 O GLY E 127 N LEU E 104
SHEET 7 AA316 VAL E 234 GLY E 239 1 O VAL E 237 N ILE E 130
SHEET 8 AA316 THR E 263 LEU E 269 1 O HIS E 267 N VAL E 236
SHEET 9 AA316 THR H 263 LEU H 269 -1 O LEU H 266 N LEU E 266
SHEET 10 AA316 VAL H 234 GLY H 239 1 N VAL H 236 O HIS H 267
SHEET 11 AA316 THR H 125 VAL H 131 1 N ILE H 130 O VAL H 237
SHEET 12 AA316 MET H 102 HIS H 107 1 N LEU H 104 O GLY H 127
SHEET 13 AA316 VAL H 27 ILE H 31 1 N ILE H 31 O VAL H 105
SHEET 14 AA316 ARG H 60 PHE H 64 1 O ARG H 60 N ILE H 28
SHEET 15 AA316 ILE H 15 GLN H 22 -1 N ILE H 20 O THR H 63
SHEET 16 AA316 VAL H 7 VAL H 12 -1 N ILE H 10 O THR H 17
SHEET 1 AA416 VAL F 7 VAL F 12 0
SHEET 2 AA416 ILE F 15 GLN F 22 -1 O THR F 17 N ILE F 10
SHEET 3 AA416 ARG F 60 PHE F 64 -1 O THR F 63 N ILE F 20
SHEET 4 AA416 VAL F 27 ILE F 31 1 N ILE F 28 O ARG F 60
SHEET 5 AA416 MET F 102 HIS F 107 1 O VAL F 105 N ILE F 31
SHEET 6 AA416 THR F 125 VAL F 131 1 O GLY F 127 N LEU F 104
SHEET 7 AA416 VAL F 234 GLY F 239 1 O VAL F 237 N ILE F 130
SHEET 8 AA416 THR F 263 LEU F 269 1 O HIS F 267 N VAL F 236
SHEET 9 AA416 THR G 263 LEU G 269 -1 O LEU G 266 N LEU F 266
SHEET 10 AA416 VAL G 234 GLY G 239 1 N VAL G 236 O HIS G 267
SHEET 11 AA416 THR G 125 VAL G 131 1 N ILE G 130 O VAL G 237
SHEET 12 AA416 MET G 102 HIS G 107 1 N LEU G 104 O GLY G 127
SHEET 13 AA416 VAL G 27 ILE G 31 1 N ILE G 31 O VAL G 105
SHEET 14 AA416 ARG G 60 PHE G 64 1 O ARG G 60 N ILE G 28
SHEET 15 AA416 ILE G 15 GLN G 22 -1 N ILE G 20 O THR G 63
SHEET 16 AA416 VAL G 7 VAL G 12 -1 N ILE G 10 O THR G 17
SHEET 1 AA516 ASN I 8 VAL I 12 0
SHEET 2 AA516 ILE I 15 GLN I 22 -1 O THR I 17 N ILE I 10
SHEET 3 AA516 ARG I 60 PHE I 64 -1 O THR I 63 N ILE I 20
SHEET 4 AA516 VAL I 27 ILE I 31 1 N ILE I 28 O ARG I 60
SHEET 5 AA516 MET I 102 HIS I 107 1 O VAL I 105 N ILE I 31
SHEET 6 AA516 THR I 125 VAL I 131 1 O GLY I 127 N LEU I 104
SHEET 7 AA516 VAL I 234 GLY I 239 1 O VAL I 237 N ILE I 130
SHEET 8 AA516 THR I 263 LEU I 269 1 O HIS I 267 N VAL I 236
SHEET 9 AA516 THR J 263 LEU J 269 -1 O LEU J 266 N LEU I 266
SHEET 10 AA516 VAL J 234 GLY J 239 1 N VAL J 236 O HIS J 267
SHEET 11 AA516 THR J 125 VAL J 131 1 N ILE J 130 O VAL J 237
SHEET 12 AA516 MET J 102 HIS J 107 1 N LEU J 104 O GLY J 127
SHEET 13 AA516 VAL J 27 ILE J 31 1 N ILE J 31 O VAL J 105
SHEET 14 AA516 ARG J 60 PHE J 64 1 O ARG J 60 N ILE J 28
SHEET 15 AA516 ILE J 15 GLN J 22 -1 N ILE J 20 O THR J 63
SHEET 16 AA516 VAL J 7 VAL J 12 -1 N ILE J 10 O THR J 17
CRYST1 176.313 244.890 192.097 90.00 90.00 90.00 C 2 2 2 80
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 0.005672 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005206 0.00000
TER 4440 SER A 298
TER 8846 SER B 298
TER 13252 SER C 298
TER 17714 SER D 298
TER 22146 SER E 298
TER 26562 SER F 298
TER 30875 SER G 298
TER 35305 SER H 298
TER 39777 SER I 298
TER 44203 SER J 298
MASTER 1088 0 1 138 80 0 0 622189 10 15 240
END |