HEADER HYDROLASE/HYDROLASE INHIBITOR 28-MAY-16 5L6A
TITLE YEAST 20S PROTEASOME WITH MOUSE BETA5I (1-138) AND MOUSE BETA6 (97-
TITLE 2 111; 118-133) IN COMPLEX WITH EPOXYKETONE INHIBITOR 17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT Y7,PROTEASOME COMPONENT Y7,PROTEINASE YSCE SUBUNIT 7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 17 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6;
COMPND 18 EC: 3.4.25.1;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 21 CHAIN: D, R;
COMPND 22 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 23 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2;
COMPND 24 EC: 3.4.25.1;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 27 CHAIN: E, S;
COMPND 28 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 29 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5;
COMPND 30 EC: 3.4.25.1;
COMPND 31 MOL_ID: 6;
COMPND 32 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 33 CHAIN: F, T;
COMPND 34 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 35 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;
COMPND 36 EC: 3.4.25.1;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 39 CHAIN: G, U;
COMPND 40 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE
COMPND 41 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,
COMPND 42 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 46 CHAIN: H, V;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 48 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 52 CHAIN: I, W;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 58 CHAIN: J, X;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-8,PROTEASOME SUBUNIT BETA
COMPND 64 TYPE-5;
COMPND 65 CHAIN: K, Y;
COMPND 66 SYNONYM: LOW MOLECULAR MASS PROTEIN 7,MACROPAIN SUBUNIT C13,
COMPND 67 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C13,PROTEASOME COMPONENT
COMPND 68 C13,PROTEASOME SUBUNIT BETA-5I,MACROPAIN SUBUNIT PRE2,MULTICATALYTIC
COMPND 69 ENDOPEPTIDASE COMPLEX SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,
COMPND 70 PROTEINASE YSCE SUBUNIT PRE2;
COMPND 71 EC: 3.4.25.1,3.4.25.1;
COMPND 72 ENGINEERED: YES;
COMPND 73 MOL_ID: 12;
COMPND 74 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6,PROTEASOME SUBUNIT BETA
COMPND 75 TYPE-1,PROTEASOME SUBUNIT BETA TYPE-6,PROTEASOME SUBUNIT BETA TYPE-1,
COMPND 76 PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 77 CHAIN: L, Z;
COMPND 78 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 79 COMPONENT C5,MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE
COMPND 80 COMPLEX SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN,
COMPND 81 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME COMPONENT
COMPND 82 C5,MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT
COMPND 83 C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN,MULTICATALYTIC
COMPND 84 ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME COMPONENT C5;
COMPND 85 EC: 3.4.25.1,3.4.25.1,3.4.25.1,3.4.25.1,3.4.25.1;
COMPND 86 ENGINEERED: YES;
COMPND 87 MOL_ID: 13;
COMPND 88 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 89 CHAIN: M, a;
COMPND 90 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 91 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 92 EC: 3.4.25.1;
COMPND 93 MOL_ID: 14;
COMPND 94 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 95 CHAIN: N, b;
COMPND 96 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 97 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 98 EC: 3.4.25.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 8 S288C);
SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 10 ORGANISM_TAXID: 559292;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 13 S288C);
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 18 S288C);
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 559292;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 23 S288C);
SOURCE 24 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 25 ORGANISM_TAXID: 559292;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 28 S288C);
SOURCE 29 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 30 ORGANISM_TAXID: 559292;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 33 S288C);
SOURCE 34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 35 ORGANISM_TAXID: 559292;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 38 S288C);
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 559292;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 43 S288C);
SOURCE 44 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 45 ORGANISM_TAXID: 559292;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 48 S288C);
SOURCE 49 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 50 ORGANISM_TAXID: 559292;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: MUS MUSCULUS, SACCHAROMYCES CEREVISIAE (STRAIN
SOURCE 53 ATCC 204508 / S288C);
SOURCE 54 ORGANISM_COMMON: MOUSE, BAKER'S YEAST;
SOURCE 55 ORGANISM_TAXID: 10090, 559292;
SOURCE 56 GENE: PSMB8, LMP7, MC13, PRE2, DOA3, PRG1, YPR103W, P8283.10;
SOURCE 57 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 58 S288C);
SOURCE 59 EXPRESSION_SYSTEM_TAXID: 559292;
SOURCE 60 MOL_ID: 12;
SOURCE 61 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 62 S288C), MUS MUSCULUS, SACCHAROMYCES CEREVISIAE;
SOURCE 63 ORGANISM_COMMON: BAKER'S YEAST, MOUSE;
SOURCE 64 ORGANISM_TAXID: 559292, 10090;
SOURCE 65 GENE: PRE7, PRS3, PTS1, YBL041W, YBL0407, PSMB1;
SOURCE 66 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 67 S288C);
SOURCE 68 EXPRESSION_SYSTEM_TAXID: 559292;
SOURCE 69 MOL_ID: 13;
SOURCE 70 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 71 S288C);
SOURCE 72 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 73 ORGANISM_TAXID: 559292;
SOURCE 74 MOL_ID: 14;
SOURCE 75 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 76 S288C);
SOURCE 77 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 78 ORGANISM_TAXID: 559292
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX, PROTEASOME, MUTANT, INHIBITOR,
KEYWDS 2 BINDING ANALYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GROLL,E.M.HUBER
REVDAT 3 10-JAN-24 5L6A 1 LINK
REVDAT 2 14-DEC-16 5L6A 1 JRNL
REVDAT 1 09-NOV-16 5L6A 0
JRNL AUTH E.M.HUBER,W.HEINEMEYER,G.DE BRUIN,H.S.OVERKLEEFT,M.GROLL
JRNL TITL A HUMANIZED YEAST PROTEASOME IDENTIFIES UNIQUE BINDING MODES
JRNL TITL 2 OF INHIBITORS FOR THE IMMUNOSUBUNIT BETA 5I.
JRNL REF EMBO J. V. 35 2602 2016
JRNL REFN ESSN 1460-2075
JRNL PMID 27789522
JRNL DOI 10.15252/EMBJ.201695222
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 239376
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12599
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17027
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 896
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 214
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.63000
REMARK 3 B22 (A**2) : -7.17000
REMARK 3 B33 (A**2) : 1.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.94000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.280
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.227
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.514
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50514 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48256 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68340 ; 0.921 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES):111122 ; 0.772 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6316 ; 4.916 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2258 ;34.077 ;24.384
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8778 ;14.134 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 290 ;14.349 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7676 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57276 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11342 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 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): 25342 ; 2.510 ; 5.752
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25341 ; 2.510 ; 5.752
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31626 ; 3.350 ; 8.614
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31627 ; 3.350 ; 8.614
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25172 ; 2.509 ; 6.175
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25172 ; 2.509 ; 6.175
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36713 ; 3.101 ; 9.105
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54350 ; 3.884 ;45.141
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54325 ; 3.875 ;45.138
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98770 ; 1.022 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 193 ;38.660 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97951 ;15.974 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 14
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A O
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 300 1
REMARK 3 1 O 1 O 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 1 A (A**2): 3795 ; 4.86 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B P
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 300 1
REMARK 3 1 P 1 P 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 2 B (A**2): 3756 ; 4.50 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 300 1
REMARK 3 1 Q 1 Q 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 3 C (A**2): 3729 ; 7.78 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 1 D 300 1
REMARK 3 1 R 1 R 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 4 D (A**2): 3578 ; 8.30 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : E S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 1 E 300 1
REMARK 3 1 S 1 S 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 5 E (A**2): 3509 ; 4.63 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : F T
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 1 F 300 1
REMARK 3 1 T 1 T 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 6 F (A**2): 3749 ; 5.58 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : G U
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 1 G 300 1
REMARK 3 1 U 1 U 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 7 G (A**2): 3770 ; 3.85 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : H V
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 1 H 300 1
REMARK 3 1 V 1 V 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 8 H (A**2): 3486 ; 3.70 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 I 1 I 300 1
REMARK 3 1 W 1 W 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 9 I (A**2): 3119 ; 2.91 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J X
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 J 1 J 300 1
REMARK 3 1 X 1 X 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 A (A): 3099 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 10 J (A**2): 3099 ; 3.53 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : K Y
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 1 K 300 1
REMARK 3 1 Y 1 Y 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 A (A): 3277 ; 0.00 ; 0.05
REMARK 3 TIGHT THERMAL 11 K (A**2): 3277 ; 2.98 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : L Z
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 300 1
REMARK 3 1 Z 1 Z 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 A (A): 3449 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 12 L (A**2): 3449 ; 4.25 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M a
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 M 1 M 300 1
REMARK 3 1 a 1 a 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 13 A (A): 3638 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 13 M (A**2): 3638 ; 3.19 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : N b
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 N 1 N 300 1
REMARK 3 1 b 1 b 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 14 A (A): 2949 ; 0.00 ; 0.05
REMARK 3 TIGHT THERMAL 14 N (A**2): 2949 ; 2.48 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
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 1 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7961 -92.2550 46.3657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0929 T22: 0.1075
REMARK 3 T33: 0.1166 T12: -0.0068
REMARK 3 T13: -0.0005 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.0281 L22: 0.0369
REMARK 3 L33: 0.0115 L12: -0.0295
REMARK 3 L13: -0.0169 L23: 0.0205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: 0.0080 S13: -0.0062
REMARK 3 S21: -0.0097 S22: 0.0055 S23: -0.0127
REMARK 3 S31: -0.0049 S32: 0.0024 S33: -0.0046
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4318 -88.0128 16.7060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0851 T22: 0.1056
REMARK 3 T33: 0.1125 T12: -0.0075
REMARK 3 T13: 0.0155 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0019 L22: 0.0068
REMARK 3 L33: 0.1284 L12: 0.0016
REMARK 3 L13: -0.0029 L23: 0.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.0019 S13: 0.0018
REMARK 3 S21: -0.0102 S22: 0.0020 S23: 0.0114
REMARK 3 S31: 0.0140 S32: 0.0132 S33: 0.0141
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1198 -87.6758 1.4922
REMARK 3 T TENSOR
REMARK 3 T11: 0.0969 T22: 0.1061
REMARK 3 T33: 0.1088 T12: 0.0002
REMARK 3 T13: -0.0042 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0004
REMARK 3 L33: 0.0007 L12: -0.0004
REMARK 3 L13: 0.0004 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: -0.0041 S13: -0.0045
REMARK 3 S21: 0.0020 S22: 0.0080 S23: 0.0027
REMARK 3 S31: 0.0013 S32: -0.0016 S33: -0.0068
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9110 -90.0006 14.0518
REMARK 3 T TENSOR
REMARK 3 T11: 0.0673 T22: 0.1032
REMARK 3 T33: 0.1197 T12: 0.0133
REMARK 3 T13: -0.0083 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: 0.0047
REMARK 3 L33: 0.0020 L12: 0.0002
REMARK 3 L13: -0.0017 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: -0.0130 S13: 0.0014
REMARK 3 S21: -0.0129 S22: -0.0013 S23: 0.0178
REMARK 3 S31: -0.0056 S32: 0.0104 S33: -0.0017
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 233
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3583 -94.3852 46.0264
REMARK 3 T TENSOR
REMARK 3 T11: 0.0253 T22: 0.1091
REMARK 3 T33: 0.1365 T12: 0.0114
REMARK 3 T13: 0.0191 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0162
REMARK 3 L33: 0.0441 L12: -0.0146
REMARK 3 L13: 0.0281 L23: -0.0213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.0014 S13: -0.0140
REMARK 3 S21: -0.0018 S22: 0.0030 S23: 0.0351
REMARK 3 S31: 0.0163 S32: -0.0006 S33: -0.0133
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0931 -95.0796 70.2155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0986 T22: 0.0964
REMARK 3 T33: 0.1185 T12: 0.0007
REMARK 3 T13: 0.0120 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0660 L22: 0.0095
REMARK 3 L33: 0.0480 L12: -0.0185
REMARK 3 L13: 0.0222 L23: -0.0152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0046 S13: -0.0084
REMARK 3 S21: 0.0013 S22: -0.0030 S23: 0.0178
REMARK 3 S31: 0.0081 S32: -0.0005 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5535 -93.5784 71.4568
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.0737
REMARK 3 T33: 0.1029 T12: -0.0096
REMARK 3 T13: -0.0064 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0128
REMARK 3 L33: 0.0088 L12: 0.0025
REMARK 3 L13: 0.0012 L23: 0.0097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0210 S13: -0.0022
REMARK 3 S21: 0.0128 S22: -0.0073 S23: -0.0050
REMARK 3 S31: -0.0004 S32: -0.0053 S33: 0.0020
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 226
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3433-129.8401 47.6091
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.0954
REMARK 3 T33: 0.1095 T12: -0.0021
REMARK 3 T13: 0.0125 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 0.0085
REMARK 3 L33: 0.0008 L12: 0.0027
REMARK 3 L13: -0.0003 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: 0.0087 S13: -0.0076
REMARK 3 S21: 0.0147 S22: -0.0053 S23: -0.0220
REMARK 3 S31: 0.0011 S32: -0.0078 S33: -0.0031
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2514-127.6200 21.2158
REMARK 3 T TENSOR
REMARK 3 T11: 0.0839 T22: 0.1119
REMARK 3 T33: 0.1147 T12: -0.0029
REMARK 3 T13: 0.0159 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0029 L22: 0.1487
REMARK 3 L33: 0.0030 L12: -0.0148
REMARK 3 L13: 0.0005 L23: -0.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: 0.0074 S13: -0.0086
REMARK 3 S21: -0.0267 S22: -0.0121 S23: -0.0117
REMARK 3 S31: -0.0097 S32: 0.0060 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3546-126.7322 -0.0527
REMARK 3 T TENSOR
REMARK 3 T11: 0.1021 T22: 0.1040
REMARK 3 T33: 0.1098 T12: -0.0047
REMARK 3 T13: 0.0110 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0427 L22: 0.0319
REMARK 3 L33: 0.0050 L12: -0.0258
REMARK 3 L13: 0.0104 L23: -0.0099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0000 S13: -0.0063
REMARK 3 S21: -0.0447 S22: -0.0003 S23: 0.0024
REMARK 3 S31: 0.0103 S32: 0.0127 S33: -0.0050
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 211
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4167-130.9559 3.3125
REMARK 3 T TENSOR
REMARK 3 T11: 0.0884 T22: 0.0969
REMARK 3 T33: 0.1095 T12: -0.0009
REMARK 3 T13: -0.0035 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.0061 L22: 0.0196
REMARK 3 L33: 0.0017 L12: 0.0099
REMARK 3 L13: 0.0022 L23: 0.0048
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: -0.0136 S13: 0.0109
REMARK 3 S21: -0.0133 S22: -0.0049 S23: 0.0264
REMARK 3 S31: 0.0032 S32: -0.0009 S33: 0.0100
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7505-134.3721 28.8933
REMARK 3 T TENSOR
REMARK 3 T11: 0.0716 T22: 0.0926
REMARK 3 T33: 0.1156 T12: 0.0040
REMARK 3 T13: 0.0132 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0058
REMARK 3 L33: 0.0112 L12: -0.0005
REMARK 3 L13: 0.0022 L23: -0.0030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0071 S13: -0.0037
REMARK 3 S21: 0.0148 S22: 0.0006 S23: 0.0203
REMARK 3 S31: -0.0111 S32: 0.0288 S33: -0.0020
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 233
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4917-137.9433 60.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0788 T22: 0.1022
REMARK 3 T33: 0.1096 T12: 0.0002
REMARK 3 T13: 0.0154 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0130 L22: 0.1308
REMARK 3 L33: 0.0031 L12: -0.0382
REMARK 3 L13: -0.0061 L23: 0.0182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: 0.0095 S13: 0.0062
REMARK 3 S21: 0.0217 S22: -0.0060 S23: 0.0098
REMARK 3 S31: -0.0031 S32: -0.0017 S33: 0.0016
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5870-134.1922 71.2467
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.0983
REMARK 3 T33: 0.0970 T12: 0.0011
REMARK 3 T13: 0.0029 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.0321 L22: 0.1707
REMARK 3 L33: 0.0054 L12: 0.0322
REMARK 3 L13: -0.0124 L23: -0.0052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: 0.0017 S13: -0.0011
REMARK 3 S21: 0.0279 S22: -0.0154 S23: 0.0013
REMARK 3 S31: -0.0001 S32: -0.0020 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4828-206.6868 37.1536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0824 T22: 0.0976
REMARK 3 T33: 0.1185 T12: -0.0099
REMARK 3 T13: -0.0067 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0031 L22: 0.0176
REMARK 3 L33: 0.0123 L12: 0.0006
REMARK 3 L13: 0.0002 L23: 0.0118
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: 0.0166 S13: 0.0007
REMARK 3 S21: -0.0107 S22: 0.0000 S23: 0.0102
REMARK 3 S31: 0.0101 S32: 0.0052 S33: 0.0070
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0806-205.6797 7.0126
REMARK 3 T TENSOR
REMARK 3 T11: 0.0887 T22: 0.0987
REMARK 3 T33: 0.1179 T12: -0.0056
REMARK 3 T13: -0.0193 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0098 L22: 0.0018
REMARK 3 L33: 0.0073 L12: 0.0015
REMARK 3 L13: -0.0068 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0081 S13: 0.0016
REMARK 3 S21: -0.0107 S22: 0.0035 S23: -0.0053
REMARK 3 S31: 0.0083 S32: 0.0091 S33: 0.0031
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0707-203.5333 -8.6815
REMARK 3 T TENSOR
REMARK 3 T11: 0.1241 T22: 0.0992
REMARK 3 T33: 0.0934 T12: 0.0116
REMARK 3 T13: -0.0083 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.0035 L22: 0.0003
REMARK 3 L33: 0.0004 L12: 0.0004
REMARK 3 L13: -0.0007 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: -0.0168 S13: 0.0074
REMARK 3 S21: 0.0012 S22: -0.0010 S23: -0.0036
REMARK 3 S31: 0.0013 S32: 0.0012 S33: -0.0032
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 ORIGIN FOR THE GROUP (A): 64.5780-203.3011 3.3548
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.0815
REMARK 3 T33: 0.1006 T12: 0.0129
REMARK 3 T13: 0.0298 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.0105 L22: 0.0134
REMARK 3 L33: 0.0055 L12: -0.0053
REMARK 3 L13: 0.0011 L23: -0.0081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: -0.0245 S13: 0.0114
REMARK 3 S21: -0.0260 S22: -0.0102 S23: -0.0284
REMARK 3 S31: 0.0162 S32: 0.0077 S33: 0.0082
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 233
REMARK 3 ORIGIN FOR THE GROUP (A): 71.6156-204.4662 35.4609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0312 T22: 0.1035
REMARK 3 T33: 0.1312 T12: 0.0251
REMARK 3 T13: -0.0043 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.0195 L22: 0.0297
REMARK 3 L33: 0.0352 L12: 0.0098
REMARK 3 L13: -0.0203 L23: 0.0068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: 0.0101 S13: 0.0054
REMARK 3 S21: 0.0179 S22: 0.0048 S23: -0.0271
REMARK 3 S31: 0.0203 S32: -0.0071 S33: -0.0091
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 244
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7106-207.9889 59.8051
REMARK 3 T TENSOR
REMARK 3 T11: 0.0995 T22: 0.0846
REMARK 3 T33: 0.1156 T12: 0.0028
REMARK 3 T13: -0.0251 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0482 L22: 0.0017
REMARK 3 L33: 0.0148 L12: 0.0072
REMARK 3 L13: -0.0166 L23: -0.0021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: -0.0129 S13: -0.0250
REMARK 3 S21: -0.0005 S22: -0.0106 S23: -0.0085
REMARK 3 S31: -0.0051 S32: -0.0185 S33: -0.0116
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3364-209.9183 61.4945
REMARK 3 T TENSOR
REMARK 3 T11: 0.1066 T22: 0.0888
REMARK 3 T33: 0.1056 T12: -0.0036
REMARK 3 T13: -0.0091 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.0239 L22: 0.0666
REMARK 3 L33: 0.0099 L12: -0.0382
REMARK 3 L13: 0.0152 L23: -0.0233
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0137 S13: 0.0013
REMARK 3 S21: 0.0165 S22: 0.0005 S23: 0.0060
REMARK 3 S31: -0.0018 S32: 0.0123 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 226
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0922-169.9357 44.9527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.1008
REMARK 3 T33: 0.1192 T12: -0.0050
REMARK 3 T13: 0.0054 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0051
REMARK 3 L33: 0.0055 L12: 0.0025
REMARK 3 L13: 0.0023 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: 0.0002 S13: 0.0045
REMARK 3 S21: 0.0187 S22: -0.0061 S23: 0.0033
REMARK 3 S31: 0.0185 S32: 0.0054 S33: -0.0043
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4265-167.5428 18.5423
REMARK 3 T TENSOR
REMARK 3 T11: 0.0683 T22: 0.1097
REMARK 3 T33: 0.1198 T12: -0.0012
REMARK 3 T13: -0.0102 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0062 L22: 0.0399
REMARK 3 L33: 0.0136 L12: 0.0117
REMARK 3 L13: -0.0030 L23: -0.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: 0.0041 S13: 0.0087
REMARK 3 S21: -0.0229 S22: 0.0004 S23: 0.0253
REMARK 3 S31: 0.0250 S32: -0.0102 S33: -0.0084
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 195
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9788-164.6641 -3.1384
REMARK 3 T TENSOR
REMARK 3 T11: 0.1174 T22: 0.0940
REMARK 3 T33: 0.1040 T12: 0.0033
REMARK 3 T13: -0.0169 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0359 L22: 0.0042
REMARK 3 L33: 0.0082 L12: -0.0092
REMARK 3 L13: -0.0154 L23: 0.0051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.0056 S13: 0.0074
REMARK 3 S21: -0.0180 S22: -0.0005 S23: -0.0016
REMARK 3 S31: -0.0163 S32: -0.0036 S33: -0.0130
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 211
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9757-161.0430 0.0910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0841 T22: 0.1020
REMARK 3 T33: 0.1202 T12: 0.0056
REMARK 3 T13: 0.0319 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: 0.0017
REMARK 3 L33: 0.0008 L12: -0.0003
REMARK 3 L13: 0.0009 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: -0.0090 S13: -0.0089
REMARK 3 S21: -0.0087 S22: 0.0096 S23: -0.0054
REMARK 3 S31: -0.0046 S32: -0.0019 S33: -0.0079
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 ORIGIN FOR THE GROUP (A): 72.7358-162.1253 25.5043
REMARK 3 T TENSOR
REMARK 3 T11: 0.0703 T22: 0.0846
REMARK 3 T33: 0.1033 T12: 0.0015
REMARK 3 T13: 0.0158 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.0051 L22: 0.0039
REMARK 3 L33: 0.0175 L12: 0.0033
REMARK 3 L13: -0.0024 L23: 0.0020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: 0.0065 S13: 0.0013
REMARK 3 S21: 0.0116 S22: 0.0014 S23: -0.0114
REMARK 3 S31: -0.0018 S32: -0.0323 S33: -0.0183
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 233
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2303-164.1361 57.7960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0847 T22: 0.0963
REMARK 3 T33: 0.1166 T12: 0.0069
REMARK 3 T13: -0.0112 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0050 L22: 0.0024
REMARK 3 L33: 0.0016 L12: -0.0012
REMARK 3 L13: -0.0023 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0156 S13: -0.0144
REMARK 3 S21: 0.0128 S22: -0.0028 S23: -0.0048
REMARK 3 S31: -0.0012 S32: -0.0123 S33: 0.0042
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4013-169.7066 68.3008
REMARK 3 T TENSOR
REMARK 3 T11: 0.1010 T22: 0.0953
REMARK 3 T33: 0.1003 T12: -0.0019
REMARK 3 T13: 0.0040 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.0433 L22: 0.1183
REMARK 3 L33: 0.0181 L12: -0.0709
REMARK 3 L13: 0.0269 L23: -0.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0027 S13: -0.0005
REMARK 3 S21: 0.0212 S22: -0.0035 S23: 0.0011
REMARK 3 S31: -0.0062 S32: -0.0086 S33: 0.0048
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5L6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1200000190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 251975
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 5CZ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, 0.1 M MES, PH
REMARK 280 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 150.26000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, 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 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 B 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
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 ILE I 126 CG1 - CB - CG2 ANGL. DEV. = -36.0 DEGREES
REMARK 500 ILE I 126 CA - CB - CG1 ANGL. DEV. = 18.4 DEGREES
REMARK 500 ARG J 95 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG J 95 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG J 95 NE - CZ - NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG J 149 CD - NE - CZ ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG J 149 NE - CZ - NH1 ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG J 149 NE - CZ - NH2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG L 100 CD - NE - CZ ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG L 100 NE - CZ - NH1 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG L 100 NE - CZ - NH2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG M 190 CG - CD - NE ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG M 190 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG M 190 NE - CZ - NH1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG M 190 NE - CZ - NH2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ILE W 126 CG1 - CB - CG2 ANGL. DEV. = -42.3 DEGREES
REMARK 500 ILE W 126 CA - CB - CG1 ANGL. DEV. = 17.5 DEGREES
REMARK 500 ARG X 95 CD - NE - CZ ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG X 95 NE - CZ - NH1 ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG X 95 NE - CZ - NH2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG X 149 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG X 149 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG X 149 NE - CZ - NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG Z 100 CD - NE - CZ ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG Z 100 NE - CZ - NH1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG Z 100 NE - CZ - NH2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG a 190 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG a 190 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG a 190 NE - CZ - NH2 ANGL. DEV. = -8.6 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
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 THR A 2 139.73 60.63
REMARK 500 TYR A 97 -65.30 -149.35
REMARK 500 ALA A 249 44.85 -95.11
REMARK 500 ARG B 8 78.49 63.67
REMARK 500 THR B 10 63.10 -115.22
REMARK 500 VAL B 51 88.69 -9.42
REMARK 500 LYS B 64 -53.33 -120.30
REMARK 500 ASN B 220 101.49 -56.07
REMARK 500 ASP B 221 -175.86 71.68
REMARK 500 PRO C 183 105.10 -45.00
REMARK 500 GLN C 202 -93.72 109.65
REMARK 500 ALA C 205 -102.46 -82.15
REMARK 500 ARG D 45 71.17 56.75
REMARK 500 SER E 39 -156.94 -112.86
REMARK 500 ASP E 137 -159.54 -124.37
REMARK 500 ASP E 202 -62.17 66.00
REMARK 500 ASP F 67 -131.43 56.39
REMARK 500 LYS F 100 -52.02 77.58
REMARK 500 ASP F 138 -167.79 -128.97
REMARK 500 SER H 171 -113.80 66.16
REMARK 500 GLN I 31 -111.33 60.15
REMARK 500 ASP I 134 -64.98 -90.69
REMARK 500 ASP I 192 30.88 -145.78
REMARK 500 GLN I 203 47.71 -105.60
REMARK 500 ASP J 2 -92.54 -105.69
REMARK 500 VAL J 9 -164.41 -102.97
REMARK 500 SER J 31 28.27 -145.70
REMARK 500 TYR K 90 48.46 -101.52
REMARK 500 ASP K 146 22.16 -79.45
REMARK 500 ASP L 32 -119.55 52.76
REMARK 500 PHE L 103 63.38 -165.82
REMARK 500 ASN L 165 73.21 54.96
REMARK 500 ASP L 200 -64.11 69.45
REMARK 500 ILE M 5 -79.82 -109.13
REMARK 500 THR M 9 -154.29 -86.90
REMARK 500 ALA M 83 -112.24 -150.22
REMARK 500 LYS N 107 -143.51 60.35
REMARK 500 THR O 2 140.01 60.58
REMARK 500 TYR O 97 -65.68 -149.30
REMARK 500 ALA O 249 44.94 -95.04
REMARK 500 ARG P 8 78.38 63.54
REMARK 500 THR P 10 63.23 -115.12
REMARK 500 VAL P 51 88.70 -9.49
REMARK 500 LYS P 64 -53.62 -120.25
REMARK 500 ASN P 220 101.59 -56.08
REMARK 500 ASP P 221 -175.82 71.65
REMARK 500 PRO Q 183 104.86 -44.95
REMARK 500 GLN Q 202 -93.63 109.70
REMARK 500 ALA Q 205 -102.58 -82.31
REMARK 500 ARG R 45 71.42 56.51
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
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 J 95 0.09 SIDE CHAIN
REMARK 500 ARG J 149 0.07 SIDE CHAIN
REMARK 500 ARG X 95 0.07 SIDE CHAIN
REMARK 500 ARG X 149 0.10 SIDE CHAIN
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 312 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B 313 DISTANCE = 6.52 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 8 OG1
REMARK 620 2 TYR G 119 O 83.9
REMARK 620 3 ARG G 122 O 82.0 82.1
REMARK 620 4 MET G 125 O 168.2 86.2 90.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 177 O
REMARK 620 2 SER I 180 O 84.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 164 O 99.6
REMARK 620 3 ASP Y 167 O 164.4 95.6
REMARK 620 4 SER Y 170 O 100.0 78.8 79.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 164 O
REMARK 620 2 ASP K 167 O 96.8
REMARK 620 3 SER K 170 O 78.8 80.0
REMARK 620 4 ASP W 204 O 100.8 160.4 95.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 99.6
REMARK 620 3 ASP V 166 O 139.0 112.7
REMARK 620 4 SER V 169 O 84.3 88.7 72.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 SER N 169 O 98.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 VAL Z 198 O 88.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 79L H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 79L K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES K 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES Y 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES b 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 79L V 301 and THR V
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 79L V 301 and THR V
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 79L Y 301 and THR Y
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 79L Y 301 and THR Y
REMARK 800 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CZ4 RELATED DB: PDB
REMARK 900 YEAST 20S PROTEASOME AT 2.3 A RESOLUTION
DBREF 5L6A A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5L6A B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5L6A C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5L6A D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5L6A E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5L6A F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5L6A G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5L6A H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5L6A I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5L6A J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5L6A K 1 138 UNP P28063 PSB8_MOUSE 73 210
DBREF 5L6A K 139 211 UNP P30656 PSB5_YEAST 215 287
DBREF 5L6A L 1 96 UNP P23724 PSB6_YEAST 20 115
DBREF 5L6A L 97 111 UNP O09061 PSB1_MOUSE 123 137
DBREF 5L6A L 112 117 UNP P23724 PSB6_YEAST 131 136
DBREF 5L6A L 118 133 UNP O09061 PSB1_MOUSE 144 159
DBREF 5L6A L 134 222 UNP P23724 PSB6_YEAST 153 241
DBREF 5L6A M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5L6A N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 5L6A O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5L6A P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5L6A Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5L6A R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5L6A S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5L6A T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5L6A U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5L6A V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5L6A W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5L6A X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5L6A Y 1 138 UNP P28063 PSB8_MOUSE 73 210
DBREF 5L6A Y 139 211 UNP P30656 PSB5_YEAST 215 287
DBREF 5L6A Z 1 96 UNP P23724 PSB6_YEAST 20 115
DBREF 5L6A Z 97 111 UNP O09061 PSB1_MOUSE 123 137
DBREF 5L6A Z 112 117 UNP P23724 PSB6_YEAST 131 136
DBREF 5L6A Z 118 133 UNP O09061 PSB1_MOUSE 144 159
DBREF 5L6A Z 134 222 UNP P23724 PSB6_YEAST 153 241
DBREF 5L6A a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5L6A b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 211 THR THR THR LEU ALA PHE LYS PHE GLN HIS GLY VAL ILE
SEQRES 2 K 211 VAL ALA VAL ASP SER ARG ALA THR ALA GLY SER TYR ILE
SEQRES 3 K 211 SER SER LEU ARG MET ASN LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 211 TYR LEU LEU GLY THR MET SER GLY CYS ALA ALA ASP CYS
SEQRES 5 K 211 GLN TYR TRP GLU ARG LEU LEU ALA LYS GLU CYS ARG LEU
SEQRES 6 K 211 TYR TYR LEU ARG ASN GLY GLU ARG ILE SER VAL SER ALA
SEQRES 7 K 211 ALA SER LYS LEU LEU SER ASN MET MET LEU GLN TYR ARG
SEQRES 8 K 211 GLY MET GLY LEU SER MET GLY SER MET ILE CYS GLY TRP
SEQRES 9 K 211 ASP LYS LYS GLY PRO GLY LEU TYR TYR VAL ASP ASP ASN
SEQRES 10 K 211 GLY THR ARG LEU SER GLY GLN MET PHE SER THR GLY SER
SEQRES 11 K 211 GLY ASN THR TYR ALA TYR GLY VAL LEU ASP SER ASN TYR
SEQRES 12 K 211 LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY
SEQRES 13 K 211 LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR
SEQRES 14 K 211 SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP
SEQRES 15 K 211 GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU
SEQRES 16 K 211 PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN
SEQRES 17 K 211 VAL ILE GLY
SEQRES 1 L 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 L 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 L 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 L 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 L 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 L 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 L 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 L 222 ASN ILE GLN HIS LEU LEU TYR SER ARG ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL TYR ASN ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 L 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 L 222 TYR GLN ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 L 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 L 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 L 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 L 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 L 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 L 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 L 222 ASP
SEQRES 1 M 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 211 THR THR THR LEU ALA PHE LYS PHE GLN HIS GLY VAL ILE
SEQRES 2 Y 211 VAL ALA VAL ASP SER ARG ALA THR ALA GLY SER TYR ILE
SEQRES 3 Y 211 SER SER LEU ARG MET ASN LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 211 TYR LEU LEU GLY THR MET SER GLY CYS ALA ALA ASP CYS
SEQRES 5 Y 211 GLN TYR TRP GLU ARG LEU LEU ALA LYS GLU CYS ARG LEU
SEQRES 6 Y 211 TYR TYR LEU ARG ASN GLY GLU ARG ILE SER VAL SER ALA
SEQRES 7 Y 211 ALA SER LYS LEU LEU SER ASN MET MET LEU GLN TYR ARG
SEQRES 8 Y 211 GLY MET GLY LEU SER MET GLY SER MET ILE CYS GLY TRP
SEQRES 9 Y 211 ASP LYS LYS GLY PRO GLY LEU TYR TYR VAL ASP ASP ASN
SEQRES 10 Y 211 GLY THR ARG LEU SER GLY GLN MET PHE SER THR GLY SER
SEQRES 11 Y 211 GLY ASN THR TYR ALA TYR GLY VAL LEU ASP SER ASN TYR
SEQRES 12 Y 211 LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY
SEQRES 13 Y 211 LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR
SEQRES 14 Y 211 SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP
SEQRES 15 Y 211 GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU
SEQRES 16 Y 211 PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN
SEQRES 17 Y 211 VAL ILE GLY
SEQRES 1 Z 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 Z 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 Z 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 Z 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 Z 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 Z 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 Z 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 Z 222 ASN ILE GLN HIS LEU LEU TYR SER ARG ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL TYR ASN ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 Z 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 Z 222 TYR GLN ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 Z 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 Z 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 Z 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 Z 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 Z 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 Z 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 Z 222 ASP
SEQRES 1 a 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
HET MG G 301 1
HET CL G 302 1
HET 79L H 301 42
HET MG I 301 1
HET MG I 302 1
HET MG J 201 1
HET 79L K 301 42
HET MG K 302 1
HET MES K 303 12
HET MG L 301 1
HET MG N 201 1
HET CL U 301 1
HET 79L V 301 42
HET 79L Y 301 42
HET MES Y 302 12
HET MG Z 301 1
HET MES b 201 12
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM 79L (2~{S})-3-(4-METHOXYPHENYL)-~{N}-[(2~{S},3~{S},4~{R})-
HETNAM 2 79L 4-METHYL-3,5-BIS(OXIDANYL)-1-PHENYL-PENTAN-2-YL]-2-
HETNAM 3 79L [[(2~{R})-2-(2-MORPHOLIN-4-YLETHANOYLAMINO)
HETNAM 4 79L PROPANOYL]AMINO]PROPANAMIDE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 29 MG 8(MG 2+)
FORMUL 30 CL 2(CL 1-)
FORMUL 31 79L 4(C31 H44 N4 O7)
FORMUL 37 MES 3(C6 H13 N O4 S)
FORMUL 46 HOH *277(H2 O)
HELIX 1 AA1 LEU A 18 GLY A 31 1 14
HELIX 2 AA2 MET A 78 SER A 96 1 19
HELIX 3 AA3 TYR A 97 GLY A 102 1 6
HELIX 4 AA4 PRO A 106 ALA A 121 1 16
HELIX 5 AA5 GLY A 167 TRP A 179 1 13
HELIX 6 AA6 GLU A 184 VAL A 200 1 17
HELIX 7 AA7 ASN A 218 LEU A 222 5 5
HELIX 8 AA8 THR A 239 ALA A 249 1 11
HELIX 9 AA9 GLY B 1 ASP B 6 5 6
HELIX 10 AB1 LEU B 18 SER B 29 1 12
HELIX 11 AB2 LEU B 79 ASN B 102 1 24
HELIX 12 AB3 PRO B 106 HIS B 124 1 19
HELIX 13 AB4 ASN B 167 TYR B 179 1 13
HELIX 14 AB5 LYS B 184 THR B 200 1 17
HELIX 15 AB6 THR B 206 ASP B 208 5 3
HELIX 16 AB7 LYS B 230 THR B 241 1 12
HELIX 17 AB8 ILE C 15 GLY C 28 1 14
HELIX 18 AB9 LEU C 76 GLU C 99 1 24
HELIX 19 AC1 THR C 103 TYR C 118 1 16
HELIX 20 AC2 ASN C 165 TYR C 177 1 13
HELIX 21 AC3 THR C 185 GLU C 199 1 15
HELIX 22 AC4 SER C 223 GLN C 239 1 17
HELIX 23 AC5 LEU D 13 LEU D 25 1 13
HELIX 24 AC6 GLU D 52 ILE D 56 5 5
HELIX 25 AC7 ASP D 76 ASP D 96 1 21
HELIX 26 AC8 ASN D 100 LEU D 113 1 14
HELIX 27 AC9 GLY D 167 TRP D 179 1 13
HELIX 28 AD1 THR D 184 MET D 200 1 17
HELIX 29 AD2 ASP D 224 ALA D 241 1 18
HELIX 30 AD3 LEU E 18 GLY E 31 1 14
HELIX 31 AD4 LEU E 76 ASN E 99 1 24
HELIX 32 AD5 ALA E 103 SER E 121 1 19
HELIX 33 AD6 ARG E 163 ILE E 179 1 17
HELIX 34 AD7 ASN E 184 SER E 197 1 14
HELIX 35 AD8 GLN E 198 LEU E 200 5 3
HELIX 36 AD9 ASP E 225 ILE E 233 5 9
HELIX 37 AE1 ASN F 17 GLY F 30 1 14
HELIX 38 AE2 LEU F 77 LYS F 100 1 24
HELIX 39 AE3 PRO F 104 HIS F 119 1 16
HELIX 40 AE4 GLY F 164 HIS F 179 1 16
HELIX 41 AE5 SER F 184 HIS F 200 1 17
HELIX 42 AE6 GLU F 201 LYS F 204 5 4
HELIX 43 AE7 LYS F 228 ASN F 244 1 17
HELIX 44 AE8 GLY G 2 HIS G 6 5 5
HELIX 45 AE9 LEU G 16 THR G 26 1 11
HELIX 46 AF1 ASN G 27 ASN G 30 5 4
HELIX 47 AF2 ASP G 56 VAL G 60 5 5
HELIX 48 AF3 PRO G 77 GLY G 100 1 24
HELIX 49 AF4 PRO G 104 ARG G 122 1 19
HELIX 50 AF5 LYS G 165 LYS G 181 1 17
HELIX 51 AF6 SER G 189 GLY G 206 1 18
HELIX 52 AF7 SER G 228 GLU G 241 1 14
HELIX 53 AF8 THR H 48 SER H 71 1 24
HELIX 54 AF9 ARG H 75 TYR H 90 1 16
HELIX 55 AG1 GLY H 130 TRP H 142 1 13
HELIX 56 AG2 THR H 147 ASP H 166 1 20
HELIX 57 AG3 ASP I 2 ILE I 6 5 5
HELIX 58 AG4 LEU I 55 GLU I 78 1 24
HELIX 59 AG5 GLU I 82 GLU I 96 1 15
HELIX 60 AG6 ALA I 141 TYR I 153 1 13
HELIX 61 AG7 GLU I 158 ASP I 175 1 18
HELIX 62 AG8 GLY J 51 ASP J 72 1 22
HELIX 63 AG9 SER J 76 ARG J 93 1 18
HELIX 64 AH1 TYR J 135 TYR J 148 1 14
HELIX 65 AH2 THR J 153 MET J 172 1 20
HELIX 66 AH3 CYS K 48 GLY K 71 1 24
HELIX 67 AH4 SER K 75 TYR K 90 1 16
HELIX 68 AH5 GLY K 131 TYR K 143 1 13
HELIX 69 AH6 SER K 148 ASP K 167 1 20
HELIX 70 AH7 VAL K 192 GLY K 204 1 13
HELIX 71 AH8 PHE L 57 HIS L 79 1 23
HELIX 72 AH9 SER L 85 SER L 99 1 15
HELIX 73 AI1 ALA L 142 VAL L 154 1 13
HELIX 74 AI2 SER L 176 HIS L 195 1 20
HELIX 75 AI3 ILE M 57 TYR M 76 1 20
HELIX 76 AI4 GLU M 88 LYS M 106 1 19
HELIX 77 AI5 GLY M 145 ARG M 156 1 12
HELIX 78 AI6 ARG M 161 ILE M 165 5 5
HELIX 79 AI7 THR M 169 ASP M 188 1 20
HELIX 80 AI8 TRP M 219 ILE M 225 5 7
HELIX 81 AI9 SER N 48 GLY N 71 1 24
HELIX 82 AJ1 SER N 74 ASN N 89 1 16
HELIX 83 AJ2 GLY N 128 PHE N 133 5 6
HELIX 84 AJ3 ILE N 134 PHE N 142 1 9
HELIX 85 AJ4 SER N 147 ASP N 166 1 20
HELIX 86 AJ5 TYR N 189 GLU N 194 1 6
HELIX 87 AJ6 LEU O 18 GLY O 31 1 14
HELIX 88 AJ7 MET O 78 SER O 96 1 19
HELIX 89 AJ8 TYR O 97 GLY O 102 1 6
HELIX 90 AJ9 PRO O 106 SER O 124 1 19
HELIX 91 AK1 GLY O 167 TRP O 179 1 13
HELIX 92 AK2 GLU O 184 VAL O 200 1 17
HELIX 93 AK3 ASN O 218 LEU O 222 5 5
HELIX 94 AK4 THR O 239 ALA O 249 1 11
HELIX 95 AK5 GLY P 1 ASP P 6 5 6
HELIX 96 AK6 LEU P 18 SER P 29 1 12
HELIX 97 AK7 LEU P 79 ASN P 102 1 24
HELIX 98 AK8 PRO P 106 HIS P 124 1 19
HELIX 99 AK9 ASN P 167 TYR P 179 1 13
HELIX 100 AL1 LYS P 184 THR P 200 1 17
HELIX 101 AL2 THR P 206 ASP P 208 5 3
HELIX 102 AL3 LYS P 230 THR P 241 1 12
HELIX 103 AL4 ILE Q 15 GLY Q 28 1 14
HELIX 104 AL5 LEU Q 76 GLU Q 99 1 24
HELIX 105 AL6 THR Q 103 TYR Q 118 1 16
HELIX 106 AL7 ASN Q 165 TYR Q 177 1 13
HELIX 107 AL8 THR Q 185 GLU Q 199 1 15
HELIX 108 AL9 SER Q 223 GLN Q 239 1 17
HELIX 109 AM1 LEU R 13 LEU R 25 1 13
HELIX 110 AM2 GLU R 52 ILE R 56 5 5
HELIX 111 AM3 ASP R 76 ASP R 96 1 21
HELIX 112 AM4 ASN R 100 LEU R 113 1 14
HELIX 113 AM5 GLY R 167 TRP R 179 1 13
HELIX 114 AM6 THR R 184 MET R 200 1 17
HELIX 115 AM7 ASP R 224 ALA R 241 1 18
HELIX 116 AM8 LEU S 18 GLY S 31 1 14
HELIX 117 AM9 LEU S 76 ASN S 99 1 24
HELIX 118 AN1 ALA S 103 SER S 121 1 19
HELIX 119 AN2 ARG S 163 ILE S 179 1 17
HELIX 120 AN3 ASN S 184 SER S 197 1 14
HELIX 121 AN4 GLN S 198 LEU S 200 5 3
HELIX 122 AN5 ASP S 225 ILE S 233 5 9
HELIX 123 AN6 ASN T 17 GLY T 30 1 14
HELIX 124 AN7 LEU T 77 LYS T 100 1 24
HELIX 125 AN8 PRO T 104 HIS T 119 1 16
HELIX 126 AN9 GLY T 164 HIS T 179 1 16
HELIX 127 AO1 SER T 184 HIS T 200 1 17
HELIX 128 AO2 GLU T 201 LYS T 204 5 4
HELIX 129 AO3 LYS T 228 ASN T 244 1 17
HELIX 130 AO4 GLY U 2 HIS U 6 5 5
HELIX 131 AO5 LEU U 16 THR U 26 1 11
HELIX 132 AO6 ASN U 27 ASN U 30 5 4
HELIX 133 AO7 ASP U 56 VAL U 60 5 5
HELIX 134 AO8 PRO U 77 GLY U 100 1 24
HELIX 135 AO9 PRO U 104 ARG U 122 1 19
HELIX 136 AP1 LYS U 165 LYS U 181 1 17
HELIX 137 AP2 SER U 189 GLY U 206 1 18
HELIX 138 AP3 SER U 228 GLU U 241 1 14
HELIX 139 AP4 THR V 48 SER V 71 1 24
HELIX 140 AP5 ARG V 75 TYR V 90 1 16
HELIX 141 AP6 GLY V 130 TRP V 142 1 13
HELIX 142 AP7 THR V 147 ASP V 166 1 20
HELIX 143 AP8 ASP W 2 ILE W 6 5 5
HELIX 144 AP9 LEU W 55 GLU W 78 1 24
HELIX 145 AQ1 GLU W 82 GLU W 96 1 15
HELIX 146 AQ2 ALA W 141 TYR W 153 1 13
HELIX 147 AQ3 GLU W 158 ASP W 175 1 18
HELIX 148 AQ4 GLY X 51 ASP X 72 1 22
HELIX 149 AQ5 SER X 76 ARG X 93 1 18
HELIX 150 AQ6 TYR X 135 TYR X 148 1 14
HELIX 151 AQ7 THR X 153 MET X 172 1 20
HELIX 152 AQ8 CYS Y 48 GLY Y 71 1 24
HELIX 153 AQ9 SER Y 75 TYR Y 90 1 16
HELIX 154 AR1 GLY Y 131 TYR Y 143 1 13
HELIX 155 AR2 SER Y 148 ASP Y 167 1 20
HELIX 156 AR3 VAL Y 192 GLY Y 204 1 13
HELIX 157 AR4 PHE Z 57 HIS Z 79 1 23
HELIX 158 AR5 SER Z 85 SER Z 99 1 15
HELIX 159 AR6 ALA Z 142 VAL Z 154 1 13
HELIX 160 AR7 SER Z 176 HIS Z 195 1 20
HELIX 161 AR8 ILE a 57 TYR a 76 1 20
HELIX 162 AR9 GLU a 88 LYS a 106 1 19
HELIX 163 AS1 GLY a 145 ARG a 156 1 12
HELIX 164 AS2 ARG a 161 ILE a 165 5 5
HELIX 165 AS3 THR a 169 ASP a 188 1 20
HELIX 166 AS4 TRP a 219 ILE a 225 5 7
HELIX 167 AS5 SER b 48 GLY b 71 1 24
HELIX 168 AS6 SER b 74 ASN b 89 1 16
HELIX 169 AS7 GLY b 128 PHE b 133 5 6
HELIX 170 AS8 ILE b 134 PHE b 142 1 9
HELIX 171 AS9 SER b 147 ASP b 166 1 20
HELIX 172 AT1 TYR b 189 GLU b 194 1 6
SHEET 1 AA1 5 ALA A 161 ILE A 164 0
SHEET 2 AA1 5 SER A 34 LYS A 38 -1 N SER A 34 O ILE A 164
SHEET 3 AA1 5 VAL A 43 GLU A 48 -1 O VAL A 44 N ILE A 37
SHEET 4 AA1 5 ILE A 209 ILE A 214 -1 O ILE A 214 N VAL A 43
SHEET 5 AA1 5 PHE A 235 LYS A 237 -1 O ARG A 236 N ILE A 213
SHEET 1 AA2 5 SER A 65 THR A 68 0
SHEET 2 AA2 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 AA2 5 VAL A 132 ASP A 140 -1 O ALA A 137 N GLY A 72
SHEET 4 AA2 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 AA2 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 AA3 6 TYR A 224 THR A 225 0
SHEET 2 AA3 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 AA3 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 AA3 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 AA3 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 AA3 6 TYR H 124 LEU H 127 -1 O LEU H 127 N ILE H 3
SHEET 1 AA4 5 ALA B 161 VAL B 164 0
SHEET 2 AA4 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 AA4 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 AA4 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 AA4 5 TYR B 225 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 AA5 5 LEU B 65 LYS B 67 0
SHEET 2 AA5 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 AA5 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 AA5 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 AA5 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 AA6 5 ALA C 159 ILE C 162 0
SHEET 2 AA6 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 AA6 5 VAL C 40 GLU C 45 -1 O VAL C 41 N VAL C 34
SHEET 4 AA6 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 AA6 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 AA7 5 SER C 63 ASP C 66 0
SHEET 2 AA7 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 AA7 5 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 AA7 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 AA7 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 AA8 5 ALA D 161 ILE D 164 0
SHEET 2 AA8 5 ALA D 29 ALA D 33 -1 N GLY D 31 O LYS D 162
SHEET 3 AA8 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 AA8 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 AA8 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 AA9 5 ILE D 59 ASP D 63 0
SHEET 2 AA9 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 AA9 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 AA9 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 AA9 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 AB1 5 GLY E 157 ILE E 160 0
SHEET 2 AB1 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 AB1 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 AB1 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 AB1 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 AB2 5 ILE E 62 ASP E 66 0
SHEET 2 AB2 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 AB2 5 VAL E 129 ASP E 137 -1 O ILE E 134 N GLY E 70
SHEET 4 AB2 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 AB2 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 AB3 5 GLY F 158 THR F 161 0
SHEET 2 AB3 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 AB3 5 GLY F 41 LEU F 49 -1 O VAL F 43 N ILE F 36
SHEET 4 AB3 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 AB3 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 AB4 5 GLN F 64 VAL F 66 0
SHEET 2 AB4 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 AB4 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 AB4 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 AB4 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 AB5 5 ALA G 159 THR G 162 0
SHEET 2 AB5 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 AB5 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 AB5 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 AB5 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
SHEET 1 AB6 5 ILE G 63 CYS G 65 0
SHEET 2 AB6 5 GLY G 71 ASN G 75 -1 O MET G 72 N PHE G 64
SHEET 3 AB6 5 ILE G 131 ASP G 138 -1 O VAL G 135 N GLY G 71
SHEET 4 AB6 5 GLY G 142 THR G 148 -1 O TYR G 146 N PHE G 134
SHEET 5 AB6 5 TYR G 154 TYR G 157 -1 O TYR G 157 N ILE G 145
SHEET 1 AB7 2 SER H 20 GLN H 22 0
SHEET 2 AB7 2 ILE H 25 ASP H 28 -1 O ILE H 25 N GLN H 22
SHEET 1 AB8 5 LEU H 34 SER H 38 0
SHEET 2 AB8 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 AB8 5 ALA H 96 ASP H 104 -1 O TYR H 97 N ALA H 46
SHEET 4 AB8 5 GLY H 107 ILE H 113 -1 O PHE H 111 N VAL H 100
SHEET 5 AB8 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 AB9 6 VAL H 212 ILE H 217 0
SHEET 2 AB9 6 GLU I 193 LEU I 199 -1 O TYR I 198 N LEU H 213
SHEET 3 AB9 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 AB9 6 VAL I 20 ASP I 25 -1 N ILE I 22 O TYR I 187
SHEET 5 AB9 6 ILE I 10 THR I 15 -1 N VAL I 12 O ALA I 23
SHEET 6 AB9 6 PHE I 135 GLY I 139 -1 O SER I 138 N VAL I 11
SHEET 1 AC1 2 LEU I 28 SER I 30 0
SHEET 2 AC1 2 LEU I 33 SER I 36 -1 O LEU I 33 N SER I 30
SHEET 1 AC2 5 ILE I 42 TYR I 45 0
SHEET 2 AC2 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 AC2 5 VAL I 104 ILE I 111 -1 O VAL I 107 N GLY I 51
SHEET 4 AC2 5 PRO I 118 PHE I 123 -1 O ALA I 121 N VAL I 108
SHEET 5 AC2 5 ILE I 129 ASP I 130 -1 O ASP I 130 N GLY I 122
SHEET 1 AC3 5 TYR J 130 ALA J 132 0
SHEET 2 AC3 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 AC3 5 SER J 12 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 AC3 5 VAL J 179 ASP J 185 -1 O VAL J 184 N VAL J 13
SHEET 5 AC3 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 AC4 2 VAL J 21 ARG J 23 0
SHEET 2 AC4 2 SER J 26 LYS J 29 -1 O SER J 26 N ARG J 23
SHEET 1 AC5 5 THR J 35 SER J 39 0
SHEET 2 AC5 5 THR J 42 GLY J 48 -1 O MET J 44 N ARG J 36
SHEET 3 AC5 5 VAL J 100 ASP J 108 -1 O GLY J 105 N LEU J 43
SHEET 4 AC5 5 LYS J 113 ILE J 119 -1 O ILE J 119 N VAL J 102
SHEET 5 AC5 5 LYS J 125 GLU J 127 -1 O VAL J 126 N GLN J 118
SHEET 1 AC6 5 MET K 125 THR K 128 0
SHEET 2 AC6 5 THR K 3 PHE K 8 -1 N ALA K 5 O PHE K 126
SHEET 3 AC6 5 GLY K 11 VAL K 16 -1 O GLY K 11 N PHE K 8
SHEET 4 AC6 5 SER K 173 THR K 180 -1 O VAL K 179 N VAL K 12
SHEET 5 AC6 5 GLY K 183 ASP K 191 -1 O HIS K 190 N VAL K 174
SHEET 1 AC7 2 ALA K 20 ALA K 22 0
SHEET 2 AC7 2 TYR K 25 SER K 28 -1 O TYR K 25 N ALA K 22
SHEET 1 AC8 4 VAL K 34 ASN K 38 0
SHEET 2 AC8 4 LEU K 41 THR K 44 -1 O LEU K 41 N ASN K 38
SHEET 3 AC8 4 MET K 97 ASP K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AC8 4 SER K 46 GLY K 47 -1 N SER K 46 O GLY K 98
SHEET 1 AC9 5 VAL K 34 ASN K 38 0
SHEET 2 AC9 5 LEU K 41 THR K 44 -1 O LEU K 41 N ASN K 38
SHEET 3 AC9 5 MET K 97 ASP K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AC9 5 GLY K 108 ASP K 115 -1 O GLY K 110 N GLY K 103
SHEET 5 AC9 5 ARG K 120 SER K 122 -1 O LEU K 121 N TYR K 113
SHEET 1 AD1 5 CYS L 136 GLY L 140 0
SHEET 2 AD1 5 THR L 11 ALA L 16 -1 N ILE L 12 O GLY L 139
SHEET 3 AD1 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AD1 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AD1 5 GLY L 211 GLU L 218 -1 O GLU L 215 N ILE L 204
SHEET 1 AD2 2 ASN L 29 THR L 31 0
SHEET 2 AD2 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AD3 5 VAL L 43 GLY L 47 0
SHEET 2 AD3 5 ILE L 50 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AD3 5 VAL L 107 LEU L 114 -1 O TYR L 108 N ASN L 55
SHEET 4 AD3 5 GLY L 120 PHE L 125 -1 O PHE L 125 N ASN L 109
SHEET 5 AD3 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD4 5 LEU M 33 PHE M 36 0
SHEET 2 AD4 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD4 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD4 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD4 5 LEU M 42 PRO M 44 -1 N ILE M 43 O VAL M 51
SHEET 1 AD5 7 LEU M 33 PHE M 36 0
SHEET 2 AD5 7 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD5 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD5 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD5 7 ASN M 112 VAL M 119 -1 O ALA M 117 N VAL M 50
SHEET 6 AD5 7 GLN M 125 ASN M 131 -1 O VAL M 130 N ILE M 114
SHEET 7 AD5 7 THR M 136 SER M 138 -1 O TYR M 137 N TYR M 129
SHEET 1 AD6 5 THR M 141 ALA M 143 0
SHEET 2 AD6 5 VAL M 11 TYR M 16 -1 N SER M 13 O LEU M 142
SHEET 3 AD6 5 GLY M 19 ASP M 25 -1 O ALA M 23 N ILE M 12
SHEET 4 AD6 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AD6 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AD7 5 TYR N 124 ALA N 127 0
SHEET 2 AD7 5 ILE N 3 PHE N 8 -1 N ALA N 5 O ALA N 125
SHEET 3 AD7 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AD7 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AD7 5 VAL N 183 PHE N 188 -1 O GLU N 184 N VAL N 177
SHEET 1 AD8 2 THR N 20 THR N 22 0
SHEET 2 AD8 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AD9 5 LEU N 34 HIS N 38 0
SHEET 2 AD9 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AD9 5 ALA N 95 TYR N 102 -1 O GLY N 96 N SER N 46
SHEET 4 AD9 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AD9 5 HIS N 120 LEU N 122 -1 O LEU N 122 N VAL N 110
SHEET 1 AE1 5 ALA O 161 ILE O 164 0
SHEET 2 AE1 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AE1 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AE1 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AE1 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AE2 5 SER O 65 THR O 68 0
SHEET 2 AE2 5 ILE O 71 GLY O 77 -1 O ALA O 73 N SER O 65
SHEET 3 AE2 5 VAL O 132 ASP O 140 -1 O ALA O 137 N GLY O 72
SHEET 4 AE2 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AE2 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AE3 6 TYR O 224 THR O 225 0
SHEET 2 AE3 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AE3 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AE3 6 GLY V 11 ASP V 17 -1 N ALA V 16 O ASP V 174
SHEET 5 AE3 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AE3 6 TYR V 124 LEU V 127 -1 O LEU V 127 N ILE V 3
SHEET 1 AE4 5 ALA P 161 VAL P 164 0
SHEET 2 AE4 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AE4 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AE4 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AE4 5 TYR P 225 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AE5 5 LEU P 65 LYS P 67 0
SHEET 2 AE5 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AE5 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AE5 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AE5 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AE6 5 ALA Q 159 ILE Q 162 0
SHEET 2 AE6 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
SHEET 3 AE6 5 VAL Q 40 GLU Q 45 -1 O VAL Q 41 N VAL Q 34
SHEET 4 AE6 5 ILE Q 208 LYS Q 214 -1 O VAL Q 213 N VAL Q 40
SHEET 5 AE6 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AE7 5 SER Q 63 ASP Q 66 0
SHEET 2 AE7 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AE7 5 VAL Q 129 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AE7 5 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AE7 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AE8 5 ALA R 161 ILE R 164 0
SHEET 2 AE8 5 ALA R 29 ALA R 33 -1 N GLY R 31 O LYS R 162
SHEET 3 AE8 5 VAL R 38 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AE8 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AE8 5 GLY R 219 ILE R 222 -1 O LYS R 221 N CYS R 213
SHEET 1 AE9 5 ILE R 59 ASP R 63 0
SHEET 2 AE9 5 ILE R 66 GLY R 72 -1 O CYS R 68 N VAL R 60
SHEET 3 AE9 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AE9 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AE9 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AF1 5 GLY S 157 ILE S 160 0
SHEET 2 AF1 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AF1 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AF1 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AF1 5 THR S 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AF2 5 ILE S 62 ASP S 66 0
SHEET 2 AF2 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AF2 5 VAL S 129 ASP S 137 -1 O ILE S 134 N GLY S 70
SHEET 4 AF2 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AF2 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AF3 5 GLY T 158 THR T 161 0
SHEET 2 AF3 5 SER T 33 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AF3 5 GLY T 41 LEU T 49 -1 O VAL T 43 N ILE T 36
SHEET 4 AF3 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AF3 5 HIS T 224 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AF4 5 GLN T 64 VAL T 66 0
SHEET 2 AF4 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AF4 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AF4 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AF4 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AF5 5 ALA U 159 THR U 162 0
SHEET 2 AF5 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AF5 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AF5 5 LEU U 214 THR U 220 -1 O GLY U 217 N VAL U 44
SHEET 5 AF5 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AF6 5 ILE U 63 CYS U 65 0
SHEET 2 AF6 5 GLY U 71 ASN U 75 -1 O MET U 72 N PHE U 64
SHEET 3 AF6 5 ILE U 131 ASP U 138 -1 O VAL U 135 N GLY U 71
SHEET 4 AF6 5 GLY U 142 THR U 148 -1 O TYR U 146 N PHE U 134
SHEET 5 AF6 5 TYR U 154 TYR U 157 -1 O TYR U 157 N ILE U 145
SHEET 1 AF7 2 SER V 20 GLN V 22 0
SHEET 2 AF7 2 ILE V 25 ASP V 28 -1 O ILE V 25 N GLN V 22
SHEET 1 AF8 5 LEU V 34 SER V 38 0
SHEET 2 AF8 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AF8 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AF8 5 GLY V 107 ILE V 113 -1 O PHE V 111 N VAL V 100
SHEET 5 AF8 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 AF9 6 VAL V 212 ILE V 217 0
SHEET 2 AF9 6 GLU W 193 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 AF9 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 AF9 6 VAL W 20 ASP W 25 -1 N ILE W 22 O TYR W 187
SHEET 5 AF9 6 ILE W 10 THR W 15 -1 N MET W 14 O ALA W 21
SHEET 6 AF9 6 PHE W 135 GLY W 139 -1 O ILE W 136 N ALA W 13
SHEET 1 AG1 2 LEU W 28 SER W 30 0
SHEET 2 AG1 2 LEU W 33 SER W 36 -1 O LEU W 33 N SER W 30
SHEET 1 AG2 5 ILE W 42 TYR W 45 0
SHEET 2 AG2 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 AG2 5 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 AG2 5 PRO W 118 PHE W 123 -1 O ALA W 121 N VAL W 108
SHEET 5 AG2 5 ILE W 129 ASP W 130 -1 O ASP W 130 N GLY W 122
SHEET 1 AG3 5 TYR X 130 ALA X 132 0
SHEET 2 AG3 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 AG3 5 SER X 12 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 AG3 5 VAL X 179 ASP X 185 -1 O VAL X 184 N VAL X 13
SHEET 5 AG3 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 AG4 2 VAL X 21 ARG X 23 0
SHEET 2 AG4 2 SER X 26 LYS X 29 -1 O SER X 26 N ARG X 23
SHEET 1 AG5 5 THR X 35 SER X 39 0
SHEET 2 AG5 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
SHEET 3 AG5 5 VAL X 100 ASP X 108 -1 O GLY X 105 N LEU X 43
SHEET 4 AG5 5 LYS X 113 ILE X 119 -1 O ILE X 119 N VAL X 102
SHEET 5 AG5 5 LYS X 125 GLU X 127 -1 O VAL X 126 N GLN X 118
SHEET 1 AG6 5 MET Y 125 THR Y 128 0
SHEET 2 AG6 5 THR Y 3 PHE Y 8 -1 N ALA Y 5 O PHE Y 126
SHEET 3 AG6 5 GLY Y 11 VAL Y 16 -1 O GLY Y 11 N PHE Y 8
SHEET 4 AG6 5 SER Y 173 THR Y 180 -1 O VAL Y 179 N VAL Y 12
SHEET 5 AG6 5 GLY Y 183 ASP Y 191 -1 O HIS Y 190 N VAL Y 174
SHEET 1 AG7 2 ALA Y 20 ALA Y 22 0
SHEET 2 AG7 2 TYR Y 25 SER Y 28 -1 O TYR Y 25 N ALA Y 22
SHEET 1 AG8 4 VAL Y 34 ASN Y 38 0
SHEET 2 AG8 4 LEU Y 41 THR Y 44 -1 O LEU Y 41 N ASN Y 38
SHEET 3 AG8 4 MET Y 97 ASP Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AG8 4 SER Y 46 GLY Y 47 -1 N SER Y 46 O GLY Y 98
SHEET 1 AG9 5 VAL Y 34 ASN Y 38 0
SHEET 2 AG9 5 LEU Y 41 THR Y 44 -1 O LEU Y 41 N ASN Y 38
SHEET 3 AG9 5 MET Y 97 ASP Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AG9 5 GLY Y 108 ASP Y 115 -1 O GLY Y 110 N GLY Y 103
SHEET 5 AG9 5 ARG Y 120 SER Y 122 -1 O LEU Y 121 N TYR Y 113
SHEET 1 AH1 5 CYS Z 136 GLY Z 140 0
SHEET 2 AH1 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 AH1 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 AH1 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 AH1 5 GLY Z 211 GLU Z 218 -1 O GLU Z 215 N ILE Z 204
SHEET 1 AH2 2 ASN Z 29 THR Z 31 0
SHEET 2 AH2 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 AH3 5 VAL Z 43 GLY Z 47 0
SHEET 2 AH3 5 ILE Z 50 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 AH3 5 VAL Z 107 LEU Z 114 -1 O TYR Z 108 N ASN Z 55
SHEET 4 AH3 5 GLY Z 120 PHE Z 125 -1 O PHE Z 125 N ASN Z 109
SHEET 5 AH3 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 AH4 5 LEU a 33 PHE a 36 0
SHEET 2 AH4 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH4 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH4 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH4 5 LEU a 42 PRO a 44 -1 N ILE a 43 O VAL a 51
SHEET 1 AH5 7 LEU a 33 PHE a 36 0
SHEET 2 AH5 7 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH5 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH5 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH5 7 ASN a 112 VAL a 119 -1 O ALA a 117 N VAL a 50
SHEET 6 AH5 7 GLN a 125 ASN a 131 -1 O VAL a 130 N ILE a 114
SHEET 7 AH5 7 THR a 136 SER a 138 -1 O TYR a 137 N TYR a 129
SHEET 1 AH6 5 THR a 141 ALA a 143 0
SHEET 2 AH6 5 VAL a 11 TYR a 16 -1 N SER a 13 O LEU a 142
SHEET 3 AH6 5 GLY a 19 ASP a 25 -1 O ALA a 23 N ILE a 12
SHEET 4 AH6 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 AH6 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 AH7 5 TYR b 124 ALA b 127 0
SHEET 2 AH7 5 ILE b 3 PHE b 8 -1 N ALA b 5 O ALA b 125
SHEET 3 AH7 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 AH7 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 AH7 5 VAL b 183 PHE b 188 -1 O GLU b 184 N VAL b 177
SHEET 1 AH8 2 THR b 20 THR b 22 0
SHEET 2 AH8 2 TYR b 25 ASN b 28 -1 O TYR b 25 N THR b 22
SHEET 1 AH9 5 LEU b 34 HIS b 38 0
SHEET 2 AH9 5 ILE b 41 GLY b 47 -1 O CYS b 43 N THR b 35
SHEET 3 AH9 5 ALA b 95 ASP b 103 -1 O GLY b 96 N SER b 46
SHEET 4 AH9 5 LYS b 107 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 AH9 5 HIS b 120 LEU b 122 -1 O LEU b 122 N VAL b 110
LINK N THR H 1 C10 79L H 301 1555 1555 1.53
LINK OG1 THR H 1 C9 79L H 301 1555 1555 1.41
LINK N THR K 1 C10 79L K 301 1555 1555 1.52
LINK OG1 THR K 1 C9 79L K 301 1555 1555 1.40
LINK N THR V 1 C10 79L V 301 1555 1555 1.53
LINK OG1 THR V 1 C9 79L V 301 1555 1555 1.41
LINK N THR Y 1 C10 79L Y 301 1555 1555 1.51
LINK OG1 THR Y 1 C9 79L Y 301 1555 1555 1.36
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.61
LINK O TYR G 119 MG MG G 301 1555 1555 2.50
LINK O ARG G 122 MG MG G 301 1555 1555 2.44
LINK O MET G 125 MG MG G 301 1555 1555 2.15
LINK O ASP I 177 MG MG I 301 1555 1555 2.32
LINK O SER I 180 MG MG I 301 1555 1555 2.53
LINK O ASP I 204 MG MG I 302 1555 1555 2.23
LINK MG MG I 302 O ALA Y 164 1555 1555 2.32
LINK MG MG I 302 O ASP Y 167 1555 1555 2.22
LINK MG MG I 302 O SER Y 170 1555 1555 2.67
LINK O ALA K 164 MG MG K 302 1555 1555 2.30
LINK O ASP K 167 MG MG K 302 1555 1555 2.15
LINK O SER K 170 MG MG K 302 1555 1555 2.69
LINK MG MG K 302 O ASP W 204 1555 1555 2.32
LINK OXT ASP L 222 MG MG L 301 1555 1555 1.97
LINK MG MG L 301 O ILE V 163 1555 1555 2.11
LINK MG MG L 301 O ASP V 166 1555 1555 2.19
LINK MG MG L 301 O SER V 169 1555 1555 2.66
LINK O ILE N 163 MG MG N 201 1555 1555 2.69
LINK O SER N 169 MG MG N 201 1555 1555 2.62
LINK O THR Z 192 MG MG Z 301 1555 1555 2.94
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.74
SITE 1 AC1 5 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 5 MET G 125
SITE 1 AC2 3 ARG G 111 ASN G 114 TYR H 69
SITE 1 AC3 14 THR H 1 ARG H 19 SER H 20 THR H 21
SITE 2 AC3 14 CYS H 31 LYS H 33 GLY H 45 ALA H 46
SITE 3 AC3 14 GLY H 47 ALA H 49 THR H 52 GLY H 168
SITE 4 AC3 14 HOH H 402 ASP I 124
SITE 1 AC4 4 ALA I 174 ASP I 177 SER I 180 ASP I 204
SITE 1 AC5 6 ASP I 204 ARG Y 19 ALA Y 164 ASP Y 167
SITE 2 AC5 6 ALA Y 168 SER Y 170
SITE 1 AC6 3 GLN J 118 ASP J 120 THR J 124
SITE 1 AC7 13 THR K 1 ARG K 19 ALA K 20 THR K 21
SITE 2 AC7 13 SER K 27 MET K 31 LYS K 33 MET K 45
SITE 3 AC7 13 GLY K 47 ALA K 49 TYR K 169 MES K 303
SITE 4 AC7 13 SER L 130
SITE 1 AC8 6 ARG K 19 ALA K 164 ASP K 167 ALA K 168
SITE 2 AC8 6 SER K 170 ASP W 204
SITE 1 AC9 3 GLY K 47 SER K 130 79L K 301
SITE 1 AD1 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 AD2 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AD2 5 LEU a 34
SITE 1 AD3 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 AD4 3 GLY Y 47 SER Y 130 79L Y 301
SITE 1 AD5 6 ARG Z 28 THR Z 192 HIS Z 195 ILE Z 196
SITE 2 AD5 6 VAL Z 198 ASP Z 222
SITE 1 AD6 6 THR b 1 SER b 46 GLY b 47 LEU b 115
SITE 2 AD6 6 GLY b 128 SER b 129
SITE 1 AD7 20 THR V 2 ILE V 3 ASP V 17 ARG V 19
SITE 2 AD7 20 SER V 20 THR V 21 CYS V 31 LYS V 33
SITE 3 AD7 20 GLY V 45 ALA V 46 GLY V 47 ALA V 49
SITE 4 AD7 20 THR V 52 GLY V 128 SER V 129 GLY V 130
SITE 5 AD7 20 GLY V 168 SER V 169 HOH V 401 ASP W 124
SITE 1 AD8 20 THR V 2 ILE V 3 ASP V 17 ARG V 19
SITE 2 AD8 20 SER V 20 THR V 21 CYS V 31 LYS V 33
SITE 3 AD8 20 GLY V 45 ALA V 46 GLY V 47 ALA V 49
SITE 4 AD8 20 THR V 52 GLY V 128 SER V 129 GLY V 130
SITE 5 AD8 20 GLY V 168 SER V 169 HOH V 401 ASP W 124
SITE 1 AD9 22 THR Y 2 THR Y 3 ASP Y 17 ARG Y 19
SITE 2 AD9 22 ALA Y 20 THR Y 21 SER Y 27 MET Y 31
SITE 3 AD9 22 LYS Y 33 MET Y 45 GLY Y 47 CYS Y 48
SITE 4 AD9 22 ALA Y 49 GLY Y 129 SER Y 130 GLY Y 131
SITE 5 AD9 22 TYR Y 169 SER Y 170 MES Y 302 SER Z 124
SITE 6 AD9 22 SER Z 130 ARG Z 137
SITE 1 AE1 22 THR Y 2 THR Y 3 ASP Y 17 ARG Y 19
SITE 2 AE1 22 ALA Y 20 THR Y 21 SER Y 27 MET Y 31
SITE 3 AE1 22 LYS Y 33 MET Y 45 GLY Y 47 CYS Y 48
SITE 4 AE1 22 ALA Y 49 GLY Y 129 SER Y 130 GLY Y 131
SITE 5 AE1 22 TYR Y 169 SER Y 170 MES Y 302 SER Z 124
SITE 6 AE1 22 SER Z 130 ARG Z 137
CRYST1 134.330 300.520 145.190 90.00 112.66 90.00 P 1 21 1 4
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 0.007444 0.000000 0.003108 0.00000
SCALE2 0.000000 0.003328 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007464 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.999627 -0.001975 0.027229 66.86262 1
MTRIX2 2 -0.002829 -0.984517 -0.175269 -289.22470 1
MTRIX3 2 0.027153 -0.175281 0.984144 -26.46655 1
(ATOM LINES ARE NOT SHOWN.)
END
