HEADER HYDROLASE/HYDROLASE INHIBITOR 15-NOV-11 3UN4
TITLE YEAST 20S PROTEASOME IN COMPLEX WITH PR-957 (MORPHOLINE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME COMPONENT Y7;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT Y7, PROTEINASE YSCE SUBUNIT 7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME COMPONENT Y13;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT Y13, PROTEINASE YSCE SUBUNIT 13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME COMPONENT PRE6;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 17 SUBUNIT PRE6, PROTEINASE YSCE SUBUNIT PRE6;
COMPND 18 EC: 3.4.25.1;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: PROTEASOME COMPONENT PUP2;
COMPND 21 CHAIN: D, R;
COMPND 22 SYNONYM: MACROPAIN SUBUNIT PUP2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 23 SUBUNIT PUP2, PROTEINASE YSCE SUBUNIT PUP2;
COMPND 24 EC: 3.4.25.1;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: PROTEASOME COMPONENT PRE5;
COMPND 27 CHAIN: E, S;
COMPND 28 SYNONYM: MACROPAIN SUBUNIT PRE5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 29 SUBUNIT PRE5, PROTEINASE YSCE SUBUNIT PRE5;
COMPND 30 EC: 3.4.25.1;
COMPND 31 MOL_ID: 6;
COMPND 32 MOLECULE: PROTEASOME COMPONENT C1;
COMPND 33 CHAIN: F, T;
COMPND 34 SYNONYM: MACROPAIN SUBUNIT C1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 35 SUBUNIT C1, PROTEINASE YSCE SUBUNIT 1;
COMPND 36 EC: 3.4.25.1;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: PROTEASOME COMPONENT C7-ALPHA;
COMPND 39 CHAIN: G, U;
COMPND 40 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, MULTICATALYTIC ENDOPEPTIDASE
COMPND 41 COMPLEX C7, PROTEASOME COMPONENT Y8, PROTEINASE YSCE SUBUNIT 7, SCL1
COMPND 42 SUPPRESSOR PROTEIN;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME COMPONENT PUP1;
COMPND 46 CHAIN: H, V;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PUP1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 48 SUBUNIT PUP1, PROTEINASE YSCE SUBUNIT PUP1;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME COMPONENT PUP3;
COMPND 52 CHAIN: I, W;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT PUP3;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME COMPONENT C11;
COMPND 58 CHAIN: J, X;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT C11, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT C11, PROTEINASE YSCE SUBUNIT 11;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME COMPONENT PRE2;
COMPND 64 CHAIN: K, Y;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT PRE2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 SUBUNIT PRE2, PROTEINASE YSCE SUBUNIT PRE2;
COMPND 67 EC: 3.4.25.1;
COMPND 68 MOL_ID: 12;
COMPND 69 MOLECULE: PROTEASOME COMPONENT C5;
COMPND 70 CHAIN: L, Z;
COMPND 71 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5;
COMPND 72 EC: 3.4.25.1;
COMPND 73 MOL_ID: 13;
COMPND 74 MOLECULE: PROTEASOME COMPONENT PRE4;
COMPND 75 CHAIN: M, a;
COMPND 76 SYNONYM: MACROPAIN SUBUNIT PRE4, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 77 SUBUNIT PRE4, PROTEINASE YSCE SUBUNIT PRE4;
COMPND 78 EC: 3.4.25.1;
COMPND 79 MOL_ID: 14;
COMPND 80 MOLECULE: PROTEASOME COMPONENT PRE3;
COMPND 81 CHAIN: N, b;
COMPND 82 SYNONYM: MACROPAIN SUBUNIT PRE3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 83 SUBUNIT PRE3, PROTEINASE YSCE SUBUNIT PRE3;
COMPND 84 EC: 3.4.25.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 559292;
SOURCE 10 STRAIN: ATCC 204508 / S288C;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 559292;
SOURCE 20 STRAIN: ATCC 204508 / S288C;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 559292;
SOURCE 25 STRAIN: ATCC 204508 / S288C;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 34 ORGANISM_TAXID: 559292;
SOURCE 35 STRAIN: ATCC 204508 / S288C;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 39 ORGANISM_TAXID: 559292;
SOURCE 40 STRAIN: ATCC 204508 / S288C;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 559292;
SOURCE 45 STRAIN: ATCC 204508 / S288C;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 559292;
SOURCE 50 STRAIN: ATCC 204508 / S288C;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 53 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 54 ORGANISM_TAXID: 559292;
SOURCE 55 STRAIN: ATCC 204508 / S288C;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 63 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 64 ORGANISM_TAXID: 559292;
SOURCE 65 STRAIN: ATCC 204508 / S288C;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 68 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 69 ORGANISM_TAXID: 559292;
SOURCE 70 STRAIN: ATCC 204508 / S288C
KEYWDS PROTEASOME, ANTIGEN PRESENTATION, DRUG DEVELOPMENT, PROTEIN
KEYWDS 2 DEGRADATION, HYDROLASE -HYDROLASE-INHIBITOR COMPLEX, HYDROLASE-
KEYWDS 3 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HUBER,M.BASLER,R.SCHWAB,W.HEINEMEYER,C.KIRK,M.GROETTRUP,M.GROLL
REVDAT 3 13-SEP-23 3UN4 1 REMARK LINK
REVDAT 2 28-MAR-12 3UN4 1 JRNL
REVDAT 1 29-FEB-12 3UN4 0
JRNL AUTH E.M.HUBER,M.BASLER,R.SCHWAB,W.HEINEMEYER,C.J.KIRK,
JRNL AUTH 2 M.GROETTRUP,M.GROLL
JRNL TITL IMMUNO- AND CONSTITUTIVE PROTEASOME CRYSTAL STRUCTURES
JRNL TITL 2 REVEAL DIFFERENCES IN SUBSTRATE AND INHIBITOR SPECIFICITY.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 148 727 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22341445
JRNL DOI 10.1016/J.CELL.2011.12.030
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 134550
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7082
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9347
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 491
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 252
REMARK 3 SOLVENT ATOMS : 1322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.86000
REMARK 3 B22 (A**2) : -8.88000
REMARK 3 B33 (A**2) : 3.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.13000
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): 0.471
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.352
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 53.346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50726 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68638 ; 0.899 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6334 ; 4.268 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2264 ;36.691 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8774 ;13.737 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 288 ;13.826 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7750 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 37954 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 50726 ; 1.302 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 430 ;40.533 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 50692 ;10.839 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 RESIDUE RANGE : A 251 A 1318
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8720 -92.3920 45.5560
REMARK 3 T TENSOR
REMARK 3 T11: 0.2325 T22: 0.1926
REMARK 3 T33: 0.2654 T12: -0.0557
REMARK 3 T13: -0.0139 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 0.7315 L22: 1.1553
REMARK 3 L33: 0.1621 L12: -0.1968
REMARK 3 L13: 0.3061 L23: -0.2005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0804 S12: 0.0003 S13: 0.0359
REMARK 3 S21: 0.0826 S22: 0.0198 S23: -0.2578
REMARK 3 S31: -0.0759 S32: -0.0457 S33: 0.0606
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 RESIDUE RANGE : B 258 B 1295
REMARK 3 ORIGIN FOR THE GROUP (A): 59.3950 -88.3160 16.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3104 T22: 0.1946
REMARK 3 T33: 0.2451 T12: -0.0667
REMARK 3 T13: 0.0396 T23: 0.0894
REMARK 3 L TENSOR
REMARK 3 L11: 0.8375 L22: 0.5782
REMARK 3 L33: 0.4594 L12: -0.0343
REMARK 3 L13: -0.0768 L23: -0.2494
REMARK 3 S TENSOR
REMARK 3 S11: -0.1876 S12: 0.0254 S13: 0.0865
REMARK 3 S21: -0.0839 S22: -0.0339 S23: -0.1413
REMARK 3 S31: -0.1243 S32: 0.0905 S33: 0.2215
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 241
REMARK 3 RESIDUE RANGE : C 253 C 1308
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1350 -87.8010 0.6110
REMARK 3 T TENSOR
REMARK 3 T11: 0.3158 T22: 0.1884
REMARK 3 T33: 0.2266 T12: 0.0147
REMARK 3 T13: -0.0219 T23: 0.0804
REMARK 3 L TENSOR
REMARK 3 L11: 0.2714 L22: 0.5677
REMARK 3 L33: 0.4032 L12: 0.2443
REMARK 3 L13: -0.3138 L23: -0.3165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: -0.0461 S13: 0.0420
REMARK 3 S21: -0.1896 S22: -0.0280 S23: 0.1016
REMARK 3 S31: -0.0417 S32: 0.0566 S33: 0.0143
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 RESIDUE RANGE : D 253 D 1314
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5630 -90.9260 14.0150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2302 T22: 0.1353
REMARK 3 T33: 0.4016 T12: 0.0936
REMARK 3 T13: -0.0581 T23: 0.1249
REMARK 3 L TENSOR
REMARK 3 L11: 0.4178 L22: 0.3810
REMARK 3 L33: 0.1389 L12: -0.0593
REMARK 3 L13: -0.2196 L23: 0.1140
REMARK 3 S TENSOR
REMARK 3 S11: -0.0793 S12: -0.0774 S13: 0.0574
REMARK 3 S21: -0.0905 S22: 0.0811 S23: 0.3075
REMARK 3 S31: -0.0192 S32: 0.0546 S33: -0.0018
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 233
REMARK 3 RESIDUE RANGE : E 234 E 1281
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7780 -94.3880 45.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.1506
REMARK 3 T33: 0.5153 T12: 0.0890
REMARK 3 T13: 0.1603 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.2298 L22: 0.7226
REMARK 3 L33: 0.3702 L12: 0.1162
REMARK 3 L13: 0.0427 L23: -0.4250
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.0324 S13: 0.1076
REMARK 3 S21: 0.1082 S22: 0.0369 S23: 0.3219
REMARK 3 S31: -0.0748 S32: 0.0071 S33: -0.0261
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 244
REMARK 3 RESIDUE RANGE : F 285 F 1321
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5380 -95.0640 69.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.5033 T22: 0.1384
REMARK 3 T33: 0.1771 T12: 0.0242
REMARK 3 T13: 0.2380 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 0.5083 L22: 0.4325
REMARK 3 L33: 0.0669 L12: -0.3322
REMARK 3 L13: 0.1681 L23: -0.1480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.0331 S13: -0.0074
REMARK 3 S21: 0.2548 S22: -0.0205 S23: 0.0982
REMARK 3 S31: -0.0498 S32: -0.0109 S33: 0.0114
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 243
REMARK 3 RESIDUE RANGE : G 244 G 1273
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6940 -93.4160 70.5650
REMARK 3 T TENSOR
REMARK 3 T11: 0.5237 T22: 0.1418
REMARK 3 T33: 0.1271 T12: -0.0375
REMARK 3 T13: -0.0658 T23: -0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 0.3572 L22: 0.6145
REMARK 3 L33: 0.1297 L12: -0.0959
REMARK 3 L13: -0.2019 L23: 0.0598
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: 0.0556 S13: -0.0075
REMARK 3 S21: 0.3758 S22: -0.0385 S23: -0.1108
REMARK 3 S31: -0.0444 S32: -0.0367 S33: 0.0350
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 RESIDUE RANGE : H 233 H 233
REMARK 3 RESIDUE RANGE : H 234 H 1288
REMARK 3 ORIGIN FOR THE GROUP (A): 67.4340-130.1970 48.1800
REMARK 3 T TENSOR
REMARK 3 T11: 0.2809 T22: 0.1634
REMARK 3 T33: 0.3422 T12: -0.0376
REMARK 3 T13: -0.1664 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.0586 L22: 0.7219
REMARK 3 L33: 0.4985 L12: -0.1414
REMARK 3 L13: -0.1568 L23: 0.4221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0608 S12: 0.0524 S13: 0.0252
REMARK 3 S21: 0.2156 S22: -0.0623 S23: -0.3460
REMARK 3 S31: -0.0659 S32: -0.0726 S33: 0.0014
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 RESIDUE RANGE : I 205 I 1322
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2130-128.0060 20.7380
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.2354
REMARK 3 T33: 0.3525 T12: -0.0339
REMARK 3 T13: 0.0774 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.2842 L22: 1.1377
REMARK 3 L33: 0.2245 L12: 0.0429
REMARK 3 L13: 0.1251 L23: 0.1023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: -0.0684 S13: -0.0479
REMARK 3 S21: 0.0600 S22: -0.0415 S23: -0.3547
REMARK 3 S31: -0.0470 S32: -0.0610 S33: 0.0316
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 198
REMARK 3 RESIDUE RANGE : J 199 J 1315
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7770-127.1310 -1.1190
REMARK 3 T TENSOR
REMARK 3 T11: 0.2418 T22: 0.2422
REMARK 3 T33: 0.1158 T12: 0.0066
REMARK 3 T13: 0.1393 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.3913 L22: 0.9712
REMARK 3 L33: 0.4141 L12: 0.0200
REMARK 3 L13: 0.3427 L23: -0.3058
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: -0.0013 S13: 0.0608
REMARK 3 S21: -0.2849 S22: -0.0412 S23: -0.0471
REMARK 3 S31: 0.0631 S32: 0.0262 S33: 0.0458
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 212
REMARK 3 RESIDUE RANGE : K 213 K 213
REMARK 3 RESIDUE RANGE : K 214 K 1313
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9090-131.4210 1.9400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1783 T22: 0.1947
REMARK 3 T33: 0.2698 T12: 0.0338
REMARK 3 T13: -0.1324 T23: 0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 0.5895 L22: 1.3351
REMARK 3 L33: 0.5773 L12: 0.3081
REMARK 3 L13: 0.0390 L23: 0.4843
REMARK 3 S TENSOR
REMARK 3 S11: -0.0582 S12: -0.0193 S13: 0.1340
REMARK 3 S21: -0.2978 S22: 0.0718 S23: 0.4641
REMARK 3 S31: -0.0696 S32: 0.0771 S33: -0.0136
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 RESIDUE RANGE : L 223 L 1302
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2210-134.6910 28.3660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1111 T22: 0.2013
REMARK 3 T33: 0.4333 T12: 0.0402
REMARK 3 T13: 0.0711 T23: 0.0509
REMARK 3 L TENSOR
REMARK 3 L11: 0.1206 L22: 0.4966
REMARK 3 L33: 0.3600 L12: -0.1617
REMARK 3 L13: 0.1142 L23: 0.0113
REMARK 3 S TENSOR
REMARK 3 S11: 0.1005 S12: -0.0085 S13: -0.0551
REMARK 3 S21: -0.1350 S22: 0.0062 S23: 0.2636
REMARK 3 S31: -0.0322 S32: -0.0051 S33: -0.1067
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 233
REMARK 3 RESIDUE RANGE : M 234 M 1312
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7830-137.9820 60.0920
REMARK 3 T TENSOR
REMARK 3 T11: 0.3201 T22: 0.1801
REMARK 3 T33: 0.2084 T12: -0.0182
REMARK 3 T13: 0.2093 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.8510 L22: 0.4797
REMARK 3 L33: 0.2309 L12: -0.0114
REMARK 3 L13: 0.4080 L23: -0.0252
REMARK 3 S TENSOR
REMARK 3 S11: 0.1844 S12: 0.0299 S13: 0.0414
REMARK 3 S21: 0.3142 S22: -0.1274 S23: 0.1452
REMARK 3 S31: 0.0261 S32: -0.0028 S33: -0.0570
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 RESIDUE RANGE : N 197 N 197
REMARK 3 RESIDUE RANGE : N 198 N 1211
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6380-134.2170 70.5860
REMARK 3 T TENSOR
REMARK 3 T11: 0.4240 T22: 0.2238
REMARK 3 T33: 0.0369 T12: -0.0192
REMARK 3 T13: 0.0607 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.6051 L22: 1.7133
REMARK 3 L33: 0.2813 L12: -0.4323
REMARK 3 L13: -0.1863 L23: -0.1558
REMARK 3 S TENSOR
REMARK 3 S11: 0.0660 S12: 0.0392 S13: 0.0955
REMARK 3 S21: 0.4180 S22: -0.0244 S23: 0.0079
REMARK 3 S31: 0.0353 S32: 0.1034 S33: -0.0417
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 RESIDUE RANGE : O 251 O 1267
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8620-206.7550 36.5500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2753 T22: 0.1181
REMARK 3 T33: 0.3699 T12: -0.0943
REMARK 3 T13: -0.1227 T23: 0.0987
REMARK 3 L TENSOR
REMARK 3 L11: 0.7371 L22: 0.8256
REMARK 3 L33: 0.3434 L12: -0.1151
REMARK 3 L13: -0.4567 L23: 0.1293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: 0.0461 S13: -0.0461
REMARK 3 S21: 0.0991 S22: 0.0474 S23: 0.2357
REMARK 3 S31: 0.1168 S32: -0.0132 S33: -0.0105
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 RESIDUE RANGE : P 258 P 1317
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5410-205.7550 6.6710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2514 T22: 0.1579
REMARK 3 T33: 0.3048 T12: 0.0091
REMARK 3 T13: -0.1532 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 0.4309 L22: 0.6111
REMARK 3 L33: 0.7848 L12: 0.4682
REMARK 3 L13: 0.3644 L23: 0.2667
REMARK 3 S TENSOR
REMARK 3 S11: 0.0449 S12: 0.0552 S13: 0.0074
REMARK 3 S21: -0.0541 S22: 0.0017 S23: 0.1243
REMARK 3 S31: 0.0801 S32: 0.0000 S33: -0.0466
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 241
REMARK 3 RESIDUE RANGE : Q 253 Q 1304
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8080-203.7900 -9.3220
REMARK 3 T TENSOR
REMARK 3 T11: 0.5111 T22: 0.1029
REMARK 3 T33: 0.3205 T12: 0.0521
REMARK 3 T13: -0.2216 T23: -0.1212
REMARK 3 L TENSOR
REMARK 3 L11: 0.0908 L22: 0.6140
REMARK 3 L33: 0.3089 L12: -0.0290
REMARK 3 L13: -0.0801 L23: 0.0275
REMARK 3 S TENSOR
REMARK 3 S11: 0.1365 S12: -0.0255 S13: -0.0808
REMARK 3 S21: -0.3480 S22: -0.0287 S23: 0.1747
REMARK 3 S31: 0.0275 S32: 0.1666 S33: -0.1078
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 RESIDUE RANGE : R 268 R 1282
REMARK 3 ORIGIN FOR THE GROUP (A): 64.5370-202.8750 4.1090
REMARK 3 T TENSOR
REMARK 3 T11: 0.3747 T22: 0.1978
REMARK 3 T33: 0.3052 T12: 0.1274
REMARK 3 T13: 0.1624 T23: -0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 0.9082 L22: 0.7941
REMARK 3 L33: 0.0892 L12: -0.2305
REMARK 3 L13: 0.2621 L23: -0.0236
REMARK 3 S TENSOR
REMARK 3 S11: 0.1119 S12: -0.1103 S13: -0.0261
REMARK 3 S21: -0.2592 S22: -0.0985 S23: -0.3300
REMARK 3 S31: 0.0454 S32: -0.0654 S33: -0.0134
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 1 S 233
REMARK 3 RESIDUE RANGE : S 234 S 1299
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4820-204.5800 35.1360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1733 T22: 0.1370
REMARK 3 T33: 0.6613 T12: 0.1033
REMARK 3 T13: -0.2335 T23: -0.0856
REMARK 3 L TENSOR
REMARK 3 L11: 1.1702 L22: 0.7090
REMARK 3 L33: 0.3511 L12: 0.7111
REMARK 3 L13: -0.1101 L23: 0.2360
REMARK 3 S TENSOR
REMARK 3 S11: 0.2091 S12: 0.1898 S13: -0.2862
REMARK 3 S21: 0.2496 S22: 0.0675 S23: -0.4887
REMARK 3 S31: 0.1023 S32: -0.0815 S33: -0.2766
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 1 T 244
REMARK 3 RESIDUE RANGE : T 285 T 1320
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6940-208.0110 59.2290
REMARK 3 T TENSOR
REMARK 3 T11: 0.4891 T22: 0.1020
REMARK 3 T33: 0.4068 T12: -0.0144
REMARK 3 T13: -0.3798 T23: 0.1139
REMARK 3 L TENSOR
REMARK 3 L11: 0.4140 L22: 0.1484
REMARK 3 L33: 0.5612 L12: 0.2146
REMARK 3 L13: -0.1701 L23: 0.0441
REMARK 3 S TENSOR
REMARK 3 S11: 0.2667 S12: -0.0415 S13: -0.2846
REMARK 3 S21: 0.2109 S22: -0.0808 S23: -0.2331
REMARK 3 S31: 0.0876 S32: -0.1503 S33: -0.1859
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 1 U 243
REMARK 3 RESIDUE RANGE : U 244 U 1310
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6180-210.0590 60.8290
REMARK 3 T TENSOR
REMARK 3 T11: 0.4291 T22: 0.1440
REMARK 3 T33: 0.2360 T12: -0.0333
REMARK 3 T13: -0.1123 T23: 0.0993
REMARK 3 L TENSOR
REMARK 3 L11: 0.2913 L22: 0.5132
REMARK 3 L33: 0.4121 L12: -0.2758
REMARK 3 L13: -0.0137 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: 0.0509 S13: -0.0353
REMARK 3 S21: 0.2521 S22: 0.0857 S23: 0.0399
REMARK 3 S31: 0.0452 S32: 0.0076 S33: -0.0539
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 RESIDUE RANGE : V 233 V 233
REMARK 3 RESIDUE RANGE : V 234 V 1307
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4050-169.9220 45.4800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1938 T22: 0.2031
REMARK 3 T33: 0.3317 T12: -0.0375
REMARK 3 T13: 0.0665 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 0.0127 L22: 1.2638
REMARK 3 L33: 0.4775 L12: 0.0802
REMARK 3 L13: -0.0108 L23: -0.4049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0548 S12: 0.0062 S13: -0.0152
REMARK 3 S21: 0.2956 S22: -0.0214 S23: 0.2714
REMARK 3 S31: 0.1129 S32: -0.0173 S33: -0.0334
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 RESIDUE RANGE : W 205 W 1316
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0910-167.5070 18.0030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1065 T22: 0.1801
REMARK 3 T33: 0.3990 T12: -0.0228
REMARK 3 T13: -0.0924 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.2817 L22: 1.2450
REMARK 3 L33: 0.3555 L12: 0.0233
REMARK 3 L13: 0.0573 L23: -0.5006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.0781 S13: -0.0634
REMARK 3 S21: -0.1256 S22: 0.0129 S23: 0.3479
REMARK 3 S31: 0.0405 S32: 0.0497 S33: -0.0324
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 198
REMARK 3 RESIDUE RANGE : X 199 X 1245
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0900-164.6910 -4.1460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3035 T22: 0.2199
REMARK 3 T33: 0.1645 T12: 0.0279
REMARK 3 T13: -0.1163 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.1409 L22: 1.0140
REMARK 3 L33: 0.1153 L12: 0.2752
REMARK 3 L13: -0.0242 L23: 0.1522
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: 0.0269 S13: -0.0490
REMARK 3 S21: -0.2573 S22: 0.0465 S23: 0.0501
REMARK 3 S31: -0.0164 S32: 0.0273 S33: 0.0062
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 212
REMARK 3 RESIDUE RANGE : Y 213 Y 213
REMARK 3 RESIDUE RANGE : Y 214 Y 1301
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0250-160.9190 -0.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.2565
REMARK 3 T33: 0.2207 T12: 0.0703
REMARK 3 T13: 0.1343 T23: -0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 0.9181 L22: 1.7792
REMARK 3 L33: 0.2628 L12: 0.6216
REMARK 3 L13: -0.0448 L23: -0.3747
REMARK 3 S TENSOR
REMARK 3 S11: 0.1523 S12: 0.0992 S13: -0.1003
REMARK 3 S21: -0.2634 S22: -0.0562 S23: -0.2185
REMARK 3 S31: 0.0138 S32: 0.0437 S33: -0.0961
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 RESIDUE RANGE : Z 223 Z 1291
REMARK 3 ORIGIN FOR THE GROUP (A): 72.6810-162.0770 25.3270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1008 T22: 0.2261
REMARK 3 T33: 0.3873 T12: 0.0737
REMARK 3 T13: 0.0391 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.2570 L22: 1.1705
REMARK 3 L33: 0.5223 L12: 0.0525
REMARK 3 L13: -0.3283 L23: 0.0479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0989 S12: 0.0531 S13: -0.0247
REMARK 3 S21: 0.0448 S22: -0.1192 S23: -0.3471
REMARK 3 S31: -0.0280 S32: -0.0467 S33: 0.0202
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 233
REMARK 3 RESIDUE RANGE : a 234 a 1287
REMARK 3 ORIGIN FOR THE GROUP (A): 61.3170-164.1280 57.3380
REMARK 3 T TENSOR
REMARK 3 T11: 0.2693 T22: 0.1592
REMARK 3 T33: 0.2229 T12: 0.0041
REMARK 3 T13: -0.1708 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.7494 L22: 0.9277
REMARK 3 L33: 0.2522 L12: -0.0568
REMARK 3 L13: 0.1871 L23: -0.3027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: 0.0640 S13: -0.0698
REMARK 3 S21: 0.3510 S22: -0.0503 S23: -0.1248
REMARK 3 S31: 0.0103 S32: 0.0126 S33: -0.0283
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 RESIDUE RANGE : b 197 b 197
REMARK 3 RESIDUE RANGE : b 198 b 1232
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6890-169.6680 67.7010
REMARK 3 T TENSOR
REMARK 3 T11: 0.4290 T22: 0.2080
REMARK 3 T33: 0.0921 T12: -0.0310
REMARK 3 T13: 0.0210 T23: 0.0869
REMARK 3 L TENSOR
REMARK 3 L11: 0.2301 L22: 1.4557
REMARK 3 L33: 0.0521 L12: 0.0085
REMARK 3 L13: 0.0535 L23: 0.1561
REMARK 3 S TENSOR
REMARK 3 S11: 0.1178 S12: 0.0360 S13: -0.0681
REMARK 3 S21: 0.3161 S22: -0.0480 S23: -0.0081
REMARK 3 S31: 0.0561 S32: -0.0612 S33: -0.0698
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK PARAMETER FOR MASK CALCULATION
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3UN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000068961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-11
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 : DOUBLE-CRYSTAL FIXED-EXIT
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 : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141633
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 12% MPD, 20 MM MGAC2, 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 150.39000
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 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 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 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
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 ILE H 223
REMARK 465 GLN H 224
REMARK 465 GLU H 225
REMARK 465 GLU H 226
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 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 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 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 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
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 ILE V 223
REMARK 465 GLN V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR N 1 C SER N 2 N 0.144
REMARK 500 THR b 1 C SER b 2 N 0.153
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR b 1 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 2 133.09 65.28
REMARK 500 SER A 53 135.70 172.85
REMARK 500 TYR A 97 -65.16 -143.80
REMARK 500 LYS A 166 -80.38 -28.73
REMARK 500 ARG B 8 70.94 57.28
REMARK 500 VAL B 51 114.55 62.15
REMARK 500 THR B 62 115.57 -160.98
REMARK 500 SER B 203 -70.16 -61.96
REMARK 500 LYS B 217 71.99 -111.51
REMARK 500 ASP B 221 -66.09 -172.38
REMARK 500 ASP C 3 18.56 -145.24
REMARK 500 ASN C 38 21.20 -140.33
REMARK 500 SER C 48 23.60 -145.01
REMARK 500 LEU C 52 24.16 174.00
REMARK 500 PRO C 183 97.72 -44.31
REMARK 500 GLN C 202 85.52 60.06
REMARK 500 THR C 203 88.99 42.12
REMARK 500 GLU C 240 29.69 -73.01
REMARK 500 ARG D 45 75.40 51.27
REMARK 500 GLU D 122 -122.26 -173.35
REMARK 500 SER E 39 -152.12 -97.18
REMARK 500 ASP E 137 -158.34 -109.17
REMARK 500 ARG E 201 -48.49 178.39
REMARK 500 GLU E 203 -165.72 -125.56
REMARK 500 LYS E 217 -65.91 -28.90
REMARK 500 GLU E 227 -39.23 -33.54
REMARK 500 ASP F 40 16.55 -143.30
REMARK 500 ASP F 67 -120.24 61.89
REMARK 500 LYS F 100 -45.57 71.51
REMARK 500 LYS F 163 -70.50 -42.34
REMARK 500 ASN F 203 24.59 -164.55
REMARK 500 ASP G 4 7.00 -66.00
REMARK 500 ASP G 40 40.17 -145.01
REMARK 500 LYS G 165 35.24 -92.48
REMARK 500 GLU G 241 45.07 -91.20
REMARK 500 GLN G 242 -34.07 -151.71
REMARK 500 ASN H 9 -35.65 -38.67
REMARK 500 ASN H 30 71.63 -153.64
REMARK 500 PRO H 105 -19.01 -46.41
REMARK 500 ASP H 145 62.95 61.45
REMARK 500 SER H 171 -116.42 66.75
REMARK 500 GLN I 31 -118.79 61.49
REMARK 500 ARG I 97 35.83 -99.10
REMARK 500 ASP I 134 -64.72 -94.02
REMARK 500 VAL J 9 -148.22 -105.84
REMARK 500 SER J 31 38.82 -143.81
REMARK 500 LYS J 34 49.15 -87.47
REMARK 500 ASP J 194 72.93 -114.98
REMARK 500 ALA J 197 76.96 -167.67
REMARK 500 SER K 18 10.06 -140.52
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR b 1 -13.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)
REMARK 630 -L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 04C H 301
REMARK 630 04C K 301
REMARK 630 04C N 201
REMARK 630 04C V 301
REMARK 630 04C Y 301
REMARK 630 04C b 201
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 00E ALA 0A1 04B
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C b 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMA RELATED DB: PDB
REMARK 900 20S PROTEASOME FROM THERMOPLASMA ACIDOPHILUM
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 20S PROTEASOME FROM YEAST
REMARK 900 RELATED ID: 1IRU RELATED DB: PDB
REMARK 900 CONSTITUTIVE 20S PROTEASOME FROM BOVINE
REMARK 900 RELATED ID: 3UN8 RELATED DB: PDB
REMARK 900 RELATED ID: 3UNH RELATED DB: PDB
REMARK 900 RELATED ID: 3UNB RELATED DB: PDB
REMARK 900 RELATED ID: 3UNF RELATED DB: PDB
REMARK 900 RELATED ID: 3UNE RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STARTING EPOXIDE RING OF AN EPOXOMICIN-LIKE INHIBITOR UNDERGOES
REMARK 999 RE-CYCLIZATION REACTION WITH THE SIDE CHAIN OF N-TERMINAL RESIDUE
REMARK 999 THR-1 (CHAINS B,N,K,V,Y AND H) AND THE FINAL PRODUCT 04C IS
REMARK 999 OBSERVED. SEE ALSO LINK RECORDS AND REMARK 630.
DBREF 3UN4 A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 3UN4 B 0 257 UNP P23638 PSA4_YEAST 1 258
DBREF 3UN4 C -1 252 UNP P40303 PSA7_YEAST 1 254
DBREF 3UN4 D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 3UN4 E 0 233 UNP P40302 PSA1_YEAST 1 234
DBREF 3UN4 F -3 284 UNP P21242 PSA3_YEAST 1 288
DBREF 3UN4 G -8 243 UNP P21243 PSA6_YEAST 1 252
DBREF 3UN4 H 1 232 UNP P25043 PSB7_YEAST 30 261
DBREF 3UN4 I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 3UN4 J 1 198 UNP P22141 PSB2_YEAST 1 198
DBREF 3UN4 K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 3UN4 L 1 222 UNP P23724 PSB1_YEAST 20 241
DBREF 3UN4 M 1 233 UNP P30657 PSB4_YEAST 34 266
DBREF 3UN4 N 1 196 UNP P38624 PSB6_YEAST 20 215
DBREF 3UN4 O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 3UN4 P 0 257 UNP P23638 PSA4_YEAST 1 258
DBREF 3UN4 Q -1 252 UNP P40303 PSA7_YEAST 1 254
DBREF 3UN4 R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 3UN4 S 0 233 UNP P40302 PSA1_YEAST 1 234
DBREF 3UN4 T -3 284 UNP P21242 PSA3_YEAST 1 288
DBREF 3UN4 U -8 243 UNP P21243 PSA6_YEAST 1 252
DBREF 3UN4 V 1 232 UNP P25043 PSB7_YEAST 30 261
DBREF 3UN4 W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 3UN4 X 1 198 UNP P22141 PSB2_YEAST 1 198
DBREF 3UN4 Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 3UN4 Z 1 222 UNP P23724 PSB1_YEAST 20 241
DBREF 3UN4 a 1 233 UNP P30657 PSB4_YEAST 34 266
DBREF 3UN4 b 1 196 UNP P38624 PSB6_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 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN 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 GLY LYS ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL HIS THR 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 GLU 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 233 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 2 M 233 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 3 M 233 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 4 M 233 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 5 M 233 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 6 M 233 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 7 M 233 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 8 M 233 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 9 M 233 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 10 M 233 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 11 M 233 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 12 M 233 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 13 M 233 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 14 M 233 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 15 M 233 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 16 M 233 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 17 M 233 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 18 M 233 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 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN 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 GLY LYS ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL HIS THR 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 GLU 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 233 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 2 a 233 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 3 a 233 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 4 a 233 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 5 a 233 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 6 a 233 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 7 a 233 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 8 a 233 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 9 a 233 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 10 a 233 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 11 a 233 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 12 a 233 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 13 a 233 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 14 a 233 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 15 a 233 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 16 a 233 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 17 a 233 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 18 a 233 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 04C H 301 42
HET 04C K 301 42
HET 04C N 201 42
HET 04C V 301 42
HET 04C Y 301 42
HET 04C b 201 42
HETNAM 04C 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-
HETNAM 2 04C ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
FORMUL 29 04C 6(C31 H44 N4 O7)
FORMUL 35 HOH *1322(H2 O)
HELIX 1 1 LEU A 18 GLY A 31 1 14
HELIX 2 2 MET A 57 LEU A 61 5 5
HELIX 3 3 MET A 78 SER A 96 1 19
HELIX 4 4 TYR A 97 GLY A 102 1 6
HELIX 5 5 PRO A 106 SER A 124 1 19
HELIX 6 6 GLY A 167 TRP A 179 1 13
HELIX 7 7 GLU A 184 GLU A 198 1 15
HELIX 8 8 ASN A 218 LEU A 222 5 5
HELIX 9 9 THR A 239 GLU A 248 1 10
HELIX 10 10 GLY B 1 ASP B 6 5 6
HELIX 11 11 LEU B 18 SER B 29 1 12
HELIX 12 12 LEU B 79 ASN B 102 1 24
HELIX 13 13 PRO B 106 HIS B 124 1 19
HELIX 14 14 ASN B 167 TYR B 179 1 13
HELIX 15 15 LYS B 184 THR B 200 1 17
HELIX 16 16 THR B 206 ASP B 208 5 3
HELIX 17 17 LYS B 230 THR B 241 1 12
HELIX 18 18 ILE C 15 GLY C 28 1 14
HELIX 19 19 LEU C 76 GLU C 99 1 24
HELIX 20 20 THR C 103 TYR C 118 1 16
HELIX 21 21 ASN C 165 LYS C 175 1 11
HELIX 22 22 THR C 185 GLN C 202 1 18
HELIX 23 23 SER C 223 GLU C 240 1 18
HELIX 24 24 LEU D 13 LYS D 24 1 12
HELIX 25 25 GLU D 52 ILE D 56 5 5
HELIX 26 26 ASP D 76 ASP D 96 1 21
HELIX 27 27 ASN D 100 LEU D 113 1 14
HELIX 28 28 GLY D 167 TRP D 179 1 13
HELIX 29 29 THR D 184 MET D 200 1 17
HELIX 30 30 ASP D 224 ALA D 240 1 17
HELIX 31 31 PHE E 1 ASP E 6 5 6
HELIX 32 32 LEU E 18 GLN E 30 1 13
HELIX 33 33 LEU E 76 ASN E 99 1 24
HELIX 34 34 ALA E 103 ASN E 118 1 16
HELIX 35 35 ARG E 163 ILE E 179 1 17
HELIX 36 36 ASN E 184 SER E 197 1 14
HELIX 37 37 GLN E 198 LEU E 200 5 3
HELIX 38 38 GLU E 227 ILE E 233 5 7
HELIX 39 39 ASN F 17 ASN F 29 1 13
HELIX 40 40 LEU F 77 LYS F 100 1 24
HELIX 41 41 PRO F 104 HIS F 119 1 16
HELIX 42 42 GLY F 164 HIS F 179 1 16
HELIX 43 43 SER F 184 HIS F 200 1 17
HELIX 44 44 GLU F 201 LYS F 204 5 4
HELIX 45 45 LYS F 228 ILE F 243 1 16
HELIX 46 46 LEU G 16 THR G 26 1 11
HELIX 47 47 PRO G 77 GLY G 100 1 24
HELIX 48 48 PRO G 104 ARG G 122 1 19
HELIX 49 49 LYS G 165 LYS G 181 1 17
HELIX 50 50 SER G 189 GLY G 206 1 18
HELIX 51 51 SER G 228 GLU G 241 1 14
HELIX 52 52 THR H 48 SER H 71 1 24
HELIX 53 53 ARG H 75 TYR H 90 1 16
HELIX 54 54 GLY H 130 TRP H 142 1 13
HELIX 55 55 THR H 147 ASP H 166 1 20
HELIX 56 56 ASP I 2 ILE I 6 5 5
HELIX 57 57 LEU I 55 GLU I 78 1 24
HELIX 58 58 GLU I 82 GLU I 96 1 15
HELIX 59 59 ALA I 141 TYR I 153 1 13
HELIX 60 60 GLU I 158 ASP I 175 1 18
HELIX 61 61 GLY J 51 ASP J 72 1 22
HELIX 62 62 SER J 76 ILE J 92 1 17
HELIX 63 63 TYR J 135 TYR J 148 1 14
HELIX 64 64 THR J 153 MET J 172 1 20
HELIX 65 65 GLY K 48 LYS K 71 1 24
HELIX 66 66 SER K 75 TYR K 90 1 16
HELIX 67 67 GLY K 132 TYR K 144 1 13
HELIX 68 68 SER K 149 ASP K 168 1 20
HELIX 69 69 VAL K 193 GLY K 205 1 13
HELIX 70 70 PHE L 57 HIS L 79 1 23
HELIX 71 71 SER L 85 GLY L 99 1 15
HELIX 72 72 ALA L 142 ASN L 155 1 14
HELIX 73 73 SER L 176 HIS L 195 1 20
HELIX 74 74 ILE M 57 TYR M 76 1 20
HELIX 75 75 GLU M 88 LYS M 106 1 19
HELIX 76 76 PHE M 146 ARG M 156 1 11
HELIX 77 77 ARG M 161 THR M 168 5 8
HELIX 78 78 THR M 169 ASP M 188 1 20
HELIX 79 79 TRP M 219 ILE M 225 5 7
HELIX 80 80 SER N 48 GLY N 71 1 24
HELIX 81 81 SER N 74 ASN N 89 1 16
HELIX 82 82 LYS N 90 LEU N 93 5 4
HELIX 83 83 GLY N 128 PHE N 133 5 6
HELIX 84 84 ILE N 134 PHE N 142 1 9
HELIX 85 85 SER N 147 ASP N 166 1 20
HELIX 86 86 TYR N 189 GLU N 194 1 6
HELIX 87 87 LEU O 18 GLY O 31 1 14
HELIX 88 88 MET O 57 LEU O 61 5 5
HELIX 89 89 MET O 78 SER O 96 1 19
HELIX 90 90 TYR O 97 GLY O 102 1 6
HELIX 91 91 PRO O 106 SER O 124 1 19
HELIX 92 92 GLY O 167 TRP O 179 1 13
HELIX 93 93 GLU O 184 GLU O 198 1 15
HELIX 94 94 ASN O 218 LEU O 222 5 5
HELIX 95 95 THR O 239 GLU O 248 1 10
HELIX 96 96 GLY P 1 ASP P 6 5 6
HELIX 97 97 LEU P 18 SER P 29 1 12
HELIX 98 98 LEU P 79 ASN P 102 1 24
HELIX 99 99 PRO P 106 HIS P 124 1 19
HELIX 100 100 ASN P 167 TYR P 179 1 13
HELIX 101 101 LYS P 184 THR P 200 1 17
HELIX 102 102 THR P 206 ASP P 208 5 3
HELIX 103 103 LYS P 230 THR P 241 1 12
HELIX 104 104 ILE Q 15 GLY Q 28 1 14
HELIX 105 105 LEU Q 76 GLU Q 99 1 24
HELIX 106 106 THR Q 103 TYR Q 118 1 16
HELIX 107 107 ASN Q 165 LYS Q 175 1 11
HELIX 108 108 THR Q 185 GLN Q 202 1 18
HELIX 109 109 SER Q 223 GLU Q 240 1 18
HELIX 110 110 LEU R 13 LYS R 24 1 12
HELIX 111 111 GLU R 52 ILE R 56 5 5
HELIX 112 112 ASP R 76 ASP R 96 1 21
HELIX 113 113 ASN R 100 LEU R 113 1 14
HELIX 114 114 GLY R 167 TRP R 179 1 13
HELIX 115 115 THR R 184 MET R 200 1 17
HELIX 116 116 ASP R 224 ALA R 240 1 17
HELIX 117 117 PHE S 1 ASP S 6 5 6
HELIX 118 118 LEU S 18 GLN S 30 1 13
HELIX 119 119 LEU S 76 ASN S 99 1 24
HELIX 120 120 ALA S 103 ASN S 118 1 16
HELIX 121 121 ARG S 163 ILE S 179 1 17
HELIX 122 122 ASN S 184 SER S 197 1 14
HELIX 123 123 GLN S 198 LEU S 200 5 3
HELIX 124 124 GLU S 227 ILE S 233 5 7
HELIX 125 125 ASN T 17 ASN T 29 1 13
HELIX 126 126 LEU T 77 LYS T 100 1 24
HELIX 127 127 PRO T 104 HIS T 119 1 16
HELIX 128 128 GLY T 164 HIS T 179 1 16
HELIX 129 129 SER T 184 HIS T 200 1 17
HELIX 130 130 GLU T 201 LYS T 204 5 4
HELIX 131 131 LYS T 228 ILE T 243 1 16
HELIX 132 132 LEU U 16 THR U 26 1 11
HELIX 133 133 PRO U 77 GLY U 100 1 24
HELIX 134 134 PRO U 104 ARG U 122 1 19
HELIX 135 135 LYS U 165 LYS U 181 1 17
HELIX 136 136 SER U 189 GLY U 206 1 18
HELIX 137 137 SER U 228 GLU U 241 1 14
HELIX 138 138 THR V 48 SER V 71 1 24
HELIX 139 139 ARG V 75 TYR V 90 1 16
HELIX 140 140 GLY V 130 TRP V 142 1 13
HELIX 141 141 THR V 147 ASP V 166 1 20
HELIX 142 142 ASP W 2 ILE W 6 5 5
HELIX 143 143 LEU W 55 GLU W 78 1 24
HELIX 144 144 GLU W 82 GLU W 96 1 15
HELIX 145 145 ALA W 141 TYR W 153 1 13
HELIX 146 146 GLU W 158 ASP W 175 1 18
HELIX 147 147 GLY X 51 ASP X 72 1 22
HELIX 148 148 SER X 76 ILE X 92 1 17
HELIX 149 149 TYR X 135 TYR X 148 1 14
HELIX 150 150 THR X 153 MET X 172 1 20
HELIX 151 151 GLY Y 48 LYS Y 71 1 24
HELIX 152 152 SER Y 75 TYR Y 90 1 16
HELIX 153 153 GLY Y 132 TYR Y 144 1 13
HELIX 154 154 SER Y 149 ASP Y 168 1 20
HELIX 155 155 VAL Y 193 GLY Y 205 1 13
HELIX 156 156 PHE Z 57 HIS Z 79 1 23
HELIX 157 157 SER Z 85 GLY Z 99 1 15
HELIX 158 158 ALA Z 142 ASN Z 155 1 14
HELIX 159 159 SER Z 176 HIS Z 195 1 20
HELIX 160 160 ILE a 57 TYR a 76 1 20
HELIX 161 161 GLU a 88 LYS a 106 1 19
HELIX 162 162 PHE a 146 ARG a 156 1 11
HELIX 163 163 ARG a 161 THR a 168 5 8
HELIX 164 164 THR a 169 ASP a 188 1 20
HELIX 165 165 TRP a 219 ILE a 225 5 7
HELIX 166 166 SER b 48 GLY b 71 1 24
HELIX 167 167 SER b 74 ASN b 89 1 16
HELIX 168 168 LYS b 90 LEU b 93 5 4
HELIX 169 169 GLY b 128 PHE b 133 5 6
HELIX 170 170 ILE b 134 PHE b 142 1 9
HELIX 171 171 SER b 147 ASP b 166 1 20
HELIX 172 172 TYR b 189 GLU b 194 1 6
SHEET 1 A 5 ALA A 161 ILE A 164 0
SHEET 2 A 5 SER A 34 LYS A 38 -1 N SER A 34 O ILE A 164
SHEET 3 A 5 VAL A 43 GLU A 48 -1 O VAL A 44 N ILE A 37
SHEET 4 A 5 ILE A 209 ILE A 214 -1 O ILE A 214 N VAL A 43
SHEET 5 A 5 PHE A 235 LYS A 237 -1 O ARG A 236 N ILE A 213
SHEET 1 B 5 SER A 65 THR A 68 0
SHEET 2 B 5 ILE A 71 GLY A 77 -1 O ILE A 71 N LEU A 67
SHEET 3 B 5 VAL A 132 ASP A 140 -1 O LEU A 135 N VAL A 74
SHEET 4 B 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 B 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 C 6 TYR A 224 THR A 225 0
SHEET 2 C 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 C 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 C 6 GLY H 11 ALA H 16 -1 N ALA H 16 O ASP H 174
SHEET 5 C 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 C 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 D 5 ALA B 161 VAL B 164 0
SHEET 2 D 5 ALA B 34 MET B 38 -1 N ALA B 34 O VAL B 164
SHEET 3 D 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 D 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 D 5 TYR B 225 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 E 5 LEU B 65 LYS B 67 0
SHEET 2 E 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 E 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 E 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 E 5 TYR B 156 GLY B 158 -1 O THR B 157 N THR B 149
SHEET 1 F 5 ALA C 159 ILE C 162 0
SHEET 2 F 5 ALA C 31 LYS C 35 -1 N ALA C 31 O ILE C 162
SHEET 3 F 5 VAL C 40 GLU C 45 -1 O GLY C 43 N VAL C 32
SHEET 4 F 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 F 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 G 5 SER C 63 ASP C 66 0
SHEET 2 G 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 G 5 VAL C 129 GLY C 135 -1 O LEU C 132 N SER C 72
SHEET 4 G 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 G 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 H 5 ALA D 161 ILE D 164 0
SHEET 2 H 5 ALA D 29 THR D 34 -1 N GLY D 31 O LYS D 162
SHEET 3 H 5 GLY D 37 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 H 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 H 5 GLY D 219 ILE D 222 -1 O GLY D 219 N THR D 215
SHEET 1 I 5 ILE D 59 GLU D 61 0
SHEET 2 I 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 I 5 VAL D 132 ASP D 140 -1 O LEU D 135 N ALA D 69
SHEET 4 I 5 GLY D 144 ALA D 150 -1 O GLN D 146 N GLY D 138
SHEET 5 I 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 J 5 GLY E 157 ILE E 160 0
SHEET 2 J 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 J 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 J 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 J 5 THR E 219 ASP E 225 -1 O TYR E 224 N ILE E 212
SHEET 1 K 5 ILE E 62 ASP E 66 0
SHEET 2 K 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 K 5 VAL E 129 ASP E 137 -1 O GLY E 130 N ALA E 74
SHEET 4 K 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 K 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 L 5 GLY F 158 THR F 161 0
SHEET 2 L 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 L 5 GLY F 41 LEU F 49 -1 O ALA F 45 N ILE F 34
SHEET 4 L 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 L 5 LYS F 225 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 M 5 GLN F 64 VAL F 66 0
SHEET 2 M 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 M 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 M 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 M 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 N 5 ALA G 159 THR G 162 0
SHEET 2 N 5 SER G 33 ARG G 37 -1 N ALA G 35 O THR G 160
SHEET 3 N 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 N 5 LEU G 214 THR G 220 -1 O ALA G 219 N THR G 42
SHEET 5 N 5 LYS G 223 THR G 226 -1 O LYS G 223 N THR G 220
SHEET 1 O 5 ILE G 63 CYS G 65 0
SHEET 2 O 5 GLY G 71 ASN G 75 -1 O MET G 72 N PHE G 64
SHEET 3 O 5 ILE G 131 ASP G 138 -1 O VAL G 135 N GLY G 71
SHEET 4 O 5 GLY G 142 THR G 148 -1 O TYR G 146 N PHE G 134
SHEET 5 O 5 TYR G 154 GLY G 156 -1 O VAL G 155 N LYS G 147
SHEET 1 P 2 SER H 20 GLN H 22 0
SHEET 2 P 2 ILE H 25 ASP H 28 -1 O ILE H 25 N GLN H 22
SHEET 1 Q 5 LEU H 34 SER H 38 0
SHEET 2 Q 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 Q 5 ALA H 96 ASP H 104 -1 O TYR H 97 N ALA H 46
SHEET 4 Q 5 GLY H 107 ILE H 113 -1 O ILE H 113 N LEU H 98
SHEET 5 Q 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 R 6 VAL H 212 ILE H 217 0
SHEET 2 R 6 VAL I 194 LEU I 199 -1 O TYR I 198 N LEU H 213
SHEET 3 R 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 R 6 CYS I 19 ASP I 25 -1 N VAL I 20 O ILE I 189
SHEET 5 R 6 ILE I 10 THR I 15 -1 N VAL I 12 O ALA I 23
SHEET 6 R 6 PHE I 135 GLY I 139 -1 O SER I 138 N VAL I 11
SHEET 1 S 2 LEU I 28 SER I 30 0
SHEET 2 S 2 LEU I 33 SER I 36 -1 O LEU I 33 N SER I 30
SHEET 1 T 5 ILE I 42 TYR I 45 0
SHEET 2 T 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 T 5 VAL I 104 ILE I 111 -1 O ALA I 109 N PHE I 49
SHEET 4 T 5 PRO I 118 PHE I 123 -1 O PHE I 119 N GLY I 110
SHEET 5 T 5 ILE I 129 ASP I 130 -1 O ASP I 130 N GLY I 122
SHEET 1 U 5 TYR J 130 HIS J 133 0
SHEET 2 U 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 U 5 VAL J 13 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 U 5 VAL J 179 ASP J 185 -1 O ILE J 180 N SER J 17
SHEET 5 U 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 V 2 VAL J 21 ARG J 23 0
SHEET 2 V 2 SER J 26 LYS J 29 -1 O SER J 26 N ARG J 23
SHEET 1 W 5 THR J 35 SER J 39 0
SHEET 2 W 5 THR J 42 GLY J 48 -1 O MET J 44 N ARG J 36
SHEET 3 W 5 VAL J 100 ASP J 108 -1 O GLY J 105 N LEU J 43
SHEET 4 W 5 LYS J 113 ILE J 119 -1 O TYR J 117 N ILE J 104
SHEET 5 W 5 LYS J 125 GLU J 127 -1 O VAL J 126 N GLN J 118
SHEET 1 X 5 ILE K 126 VAL K 129 0
SHEET 2 X 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 129
SHEET 3 X 5 GLY K 11 VAL K 16 -1 O GLY K 11 N PHE K 8
SHEET 4 X 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 X 5 GLY K 184 ASP K 192 -1 O HIS K 188 N LEU K 177
SHEET 1 Y 2 ALA K 20 ALA K 22 0
SHEET 2 Y 2 TRP K 25 SER K 28 -1 O TRP K 25 N ALA K 22
SHEET 1 Z 5 VAL K 34 ASN K 38 0
SHEET 2 Z 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 Z 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 Z 5 GLY K 109 ASP K 116 -1 O VAL K 115 N THR K 99
SHEET 5 Z 5 ARG K 121 GLY K 124 -1 O LEU K 122 N TYR K 114
SHEET 1 AA 5 CYS L 136 GLY L 140 0
SHEET 2 AA 5 THR L 11 ALA L 16 -1 N ILE L 12 O GLY L 139
SHEET 3 AA 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AA 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AA 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AB 2 ASN L 29 THR L 31 0
SHEET 2 AB 2 SER L 34 SER L 37 -1 O SER L 34 N THR L 31
SHEET 1 AC 5 PHE L 44 GLY L 47 0
SHEET 2 AC 5 ILE L 50 GLY L 56 -1 O ILE L 50 N CYS L 46
SHEET 3 AC 5 VAL L 107 LEU L 114 -1 O HIS L 108 N ASN L 55
SHEET 4 AC 5 GLY L 120 PHE L 125 -1 O TYR L 123 N ILE L 111
SHEET 5 AC 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD 5 LEU M 33 PHE M 36 0
SHEET 2 AD 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD 5 LEU M 42 VAL M 45 -1 N ILE M 43 O VAL M 51
SHEET 1 AE 7 LEU M 33 PHE M 36 0
SHEET 2 AE 7 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AE 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AE 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AE 7 ASN M 112 VAL M 119 -1 O ALA M 117 N VAL M 50
SHEET 6 AE 7 GLN M 125 ASN M 131 -1 O PHE M 126 N GLY M 118
SHEET 7 AE 7 THR M 136 TYR M 137 -1 O TYR M 137 N TYR M 129
SHEET 1 AF 5 THR M 141 ALA M 143 0
SHEET 2 AF 5 VAL M 11 LYS M 15 -1 N SER M 13 O LEU M 142
SHEET 3 AF 5 GLY M 19 ASP M 25 -1 O ALA M 23 N ILE M 12
SHEET 4 AF 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AF 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 PHE N 8 -1 N ILE N 3 O ALA N 127
SHEET 3 AG 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AG 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AG 5 GLY N 182 PHE N 188 -1 O LEU N 186 N MET N 175
SHEET 1 AH 2 THR N 20 THR N 22 0
SHEET 2 AH 2 TYR N 25 ASN N 28 -1 O ASN N 28 N THR N 20
SHEET 1 AI 5 LEU N 34 HIS N 38 0
SHEET 2 AI 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AI 5 ALA N 95 ASP N 103 -1 O ALA N 100 N TRP N 42
SHEET 4 AI 5 LYS N 107 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AI 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AJ 5 ALA O 161 ILE O 164 0
SHEET 2 AJ 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AJ 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AJ 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AJ 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AK 5 SER O 65 THR O 68 0
SHEET 2 AK 5 ILE O 71 GLY O 77 -1 O ILE O 71 N LEU O 67
SHEET 3 AK 5 VAL O 132 ASP O 140 -1 O LEU O 135 N VAL O 74
SHEET 4 AK 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AK 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AL 6 TYR O 224 THR O 225 0
SHEET 2 AL 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AL 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AL 6 GLY V 11 ALA V 16 -1 N ALA V 16 O ASP V 174
SHEET 5 AL 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AL 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AM 5 ALA P 161 VAL P 164 0
SHEET 2 AM 5 ALA P 34 MET P 38 -1 N GLY P 36 O ILE P 162
SHEET 3 AM 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AM 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AM 5 TYR P 225 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AN 5 LEU P 65 LYS P 67 0
SHEET 2 AN 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AN 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AN 5 GLY P 144 SER P 150 -1 O GLN P 146 N GLY P 138
SHEET 5 AN 5 TYR P 156 GLY P 158 -1 O THR P 157 N THR P 149
SHEET 1 AO 5 ALA Q 159 ILE Q 162 0
SHEET 2 AO 5 ALA Q 31 LYS Q 35 -1 N ALA Q 31 O ILE Q 162
SHEET 3 AO 5 VAL Q 40 GLU Q 45 -1 O GLY Q 43 N VAL Q 32
SHEET 4 AO 5 ILE Q 208 LYS Q 214 -1 O VAL Q 213 N VAL Q 40
SHEET 5 AO 5 ASP Q 218 ALA Q 221 -1 O VAL Q 220 N VAL Q 212
SHEET 1 AP 5 SER Q 63 ASP Q 66 0
SHEET 2 AP 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AP 5 VAL Q 129 GLY Q 135 -1 O LEU Q 132 N SER Q 72
SHEET 4 AP 5 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AP 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AQ 5 ALA R 161 ILE R 164 0
SHEET 2 AQ 5 ALA R 29 THR R 34 -1 N GLY R 31 O LYS R 162
SHEET 3 AQ 5 GLY R 37 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AQ 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AQ 5 GLY R 219 ILE R 222 -1 O GLY R 219 N THR R 215
SHEET 1 AR 5 ILE R 59 ASP R 63 0
SHEET 2 AR 5 ILE R 66 GLY R 72 -1 O ILE R 66 N ASP R 63
SHEET 3 AR 5 VAL R 132 ASP R 140 -1 O LEU R 135 N ALA R 69
SHEET 4 AR 5 GLY R 144 ALA R 150 -1 O GLN R 146 N GLY R 138
SHEET 5 AR 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AS 5 GLY S 157 ILE S 160 0
SHEET 2 AS 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AS 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AS 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AS 5 THR S 219 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AT 5 ILE S 62 ASP S 66 0
SHEET 2 AT 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AT 5 VAL S 129 ASP S 137 -1 O GLY S 130 N ALA S 74
SHEET 4 AT 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AT 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AU 5 GLY T 158 THR T 161 0
SHEET 2 AU 5 SER T 33 LYS T 37 -1 N GLY T 35 O ALA T 159
SHEET 3 AU 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AU 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AU 5 LYS T 225 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AV 5 GLN T 64 VAL T 66 0
SHEET 2 AV 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AV 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AV 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AV 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AW 5 ALA U 159 THR U 162 0
SHEET 2 AW 5 SER U 33 ARG U 37 -1 N ALA U 35 O THR U 160
SHEET 3 AW 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AW 5 LEU U 214 THR U 220 -1 O ALA U 219 N THR U 42
SHEET 5 AW 5 LYS U 223 THR U 226 -1 O LYS U 223 N THR U 220
SHEET 1 AX 5 ILE U 63 CYS U 65 0
SHEET 2 AX 5 GLY U 71 ASN U 75 -1 O MET U 72 N PHE U 64
SHEET 3 AX 5 ILE U 131 ASP U 138 -1 O VAL U 135 N GLY U 71
SHEET 4 AX 5 GLY U 142 THR U 148 -1 O TYR U 146 N PHE U 134
SHEET 5 AX 5 TYR U 154 GLY U 156 -1 O VAL U 155 N LYS U 147
SHEET 1 AY 2 SER V 20 GLN V 22 0
SHEET 2 AY 2 ILE V 25 ASP V 28 -1 O ILE V 25 N GLN V 22
SHEET 1 AZ 5 LEU V 34 SER V 38 0
SHEET 2 AZ 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AZ 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AZ 5 GLY V 107 ILE V 113 -1 O ILE V 113 N LEU V 98
SHEET 5 AZ 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 BA 6 VAL V 212 ILE V 217 0
SHEET 2 BA 6 VAL W 194 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 BA 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 BA 6 CYS W 19 ASP W 25 -1 N VAL W 20 O ILE W 189
SHEET 5 BA 6 ILE W 10 THR W 15 -1 N VAL W 12 O ALA W 23
SHEET 6 BA 6 PHE W 135 GLY W 139 -1 O SER W 138 N VAL W 11
SHEET 1 BB 2 LEU W 28 SER W 30 0
SHEET 2 BB 2 LEU W 33 SER W 36 -1 O LEU W 33 N SER W 30
SHEET 1 BC 5 ILE W 42 TYR W 45 0
SHEET 2 BC 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 BC 5 VAL W 104 ILE W 111 -1 O ALA W 109 N PHE W 49
SHEET 4 BC 5 PRO W 118 PHE W 123 -1 O PHE W 119 N GLY W 110
SHEET 5 BC 5 ILE W 129 ASP W 130 -1 O ASP W 130 N GLY W 122
SHEET 1 BD 5 TYR X 130 HIS X 133 0
SHEET 2 BD 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 BD 5 VAL X 13 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O ILE X 180 N SER X 17
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 BE 2 VAL X 21 ARG X 23 0
SHEET 2 BE 2 SER X 26 LYS X 29 -1 O SER X 26 N ARG X 23
SHEET 1 BF 5 THR X 35 SER X 39 0
SHEET 2 BF 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
SHEET 3 BF 5 VAL X 100 ASP X 108 -1 O ASN X 101 N ALA X 47
SHEET 4 BF 5 LYS X 113 ILE X 119 -1 O TYR X 117 N ILE X 104
SHEET 5 BF 5 LYS X 125 GLU X 127 -1 O VAL X 126 N GLN X 118
SHEET 1 BG 5 ILE Y 126 VAL Y 129 0
SHEET 2 BG 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O GLY Y 11 N PHE Y 8
SHEET 4 BG 5 SER Y 174 THR Y 181 -1 O VAL Y 180 N ILE Y 12
SHEET 5 BG 5 GLY Y 184 ASP Y 192 -1 O HIS Y 188 N LEU Y 177
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 BI 5 VAL Y 34 ASN Y 38 0
SHEET 2 BI 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BI 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BI 5 GLY Y 109 ASP Y 116 -1 O VAL Y 115 N THR Y 99
SHEET 5 BI 5 ARG Y 121 GLY Y 124 -1 O LEU Y 122 N TYR Y 114
SHEET 1 BJ 5 CYS Z 136 GLY Z 140 0
SHEET 2 BJ 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 BJ 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 BJ 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 BJ 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 BK 2 ASN Z 29 THR Z 31 0
SHEET 2 BK 2 SER Z 34 SER Z 37 -1 O SER Z 37 N ASN Z 29
SHEET 1 BL 5 PHE Z 44 GLY Z 47 0
SHEET 2 BL 5 ILE Z 50 GLY Z 56 -1 O ILE Z 50 N CYS Z 46
SHEET 3 BL 5 VAL Z 107 LEU Z 114 -1 O HIS Z 108 N ASN Z 55
SHEET 4 BL 5 GLY Z 120 PHE Z 125 -1 O TYR Z 123 N ILE Z 111
SHEET 5 BL 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 BM 5 LEU a 33 PHE a 36 0
SHEET 2 BM 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 BM 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 BM 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 BM 5 LEU a 42 VAL a 45 -1 N ILE a 43 O VAL a 51
SHEET 1 BN 7 LEU a 33 PHE a 36 0
SHEET 2 BN 7 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 BN 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 BN 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 BN 7 ASN a 112 VAL a 119 -1 O ALA a 117 N VAL a 50
SHEET 6 BN 7 GLN a 125 ASN a 131 -1 O PHE a 126 N GLY a 118
SHEET 7 BN 7 THR a 136 TYR a 137 -1 O TYR a 137 N TYR a 129
SHEET 1 BO 5 THR a 141 ALA a 143 0
SHEET 2 BO 5 VAL a 11 LYS a 15 -1 N SER a 13 O LEU a 142
SHEET 3 BO 5 GLY a 19 ASP a 25 -1 O ALA a 23 N ILE a 12
SHEET 4 BO 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 BO 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 BP 5 TYR b 124 ALA b 127 0
SHEET 2 BP 5 ILE b 3 PHE b 8 -1 N ILE b 3 O ALA b 127
SHEET 3 BP 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 BP 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 BP 5 GLY b 182 PHE b 188 -1 O LEU b 186 N MET b 175
SHEET 1 BQ 2 THR b 20 THR b 22 0
SHEET 2 BQ 2 TYR b 25 ASN b 28 -1 O ASN b 28 N THR b 20
SHEET 1 BR 5 LEU b 34 HIS b 38 0
SHEET 2 BR 5 ILE b 41 GLY b 47 -1 O CYS b 43 N THR b 35
SHEET 3 BR 5 ALA b 95 ASP b 103 -1 O ALA b 100 N TRP b 42
SHEET 4 BR 5 LYS b 107 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 BR 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR H 1 C9 04C H 301 1555 1555 1.46
LINK N THR H 1 C10 04C H 301 1555 1555 1.51
LINK OG1 THR K 1 C9 04C K 301 1555 1555 1.45
LINK N THR K 1 C10 04C K 301 1555 1555 1.50
LINK OG1 THR N 1 C9 04C N 201 1555 1555 1.44
LINK N THR N 1 C10 04C N 201 1555 1555 1.52
LINK OG1 THR V 1 C9 04C V 301 1555 1555 1.45
LINK N THR V 1 C10 04C V 301 1555 1555 1.52
LINK OG1 THR Y 1 C9 04C Y 301 1555 1555 1.45
LINK N THR Y 1 C10 04C Y 301 1555 1555 1.51
LINK OG1 THR b 1 C9 04C b 201 1555 1555 1.44
LINK N THR b 1 C10 04C b 201 1555 1555 1.53
SITE 1 AC1 15 THR H 1 ARG H 19 SER H 20 THR H 21
SITE 2 AC1 15 CYS H 31 LYS H 33 GLY H 45 GLY H 47
SITE 3 AC1 15 THR H 48 ALA H 49 THR H 52 GLY H 168
SITE 4 AC1 15 HOH H 442 ASP I 124 ILE I 126
SITE 1 AC2 13 THR K 1 ARG K 19 ALA K 20 THR K 21
SITE 2 AC2 13 VAL K 31 LYS K 33 MET K 45 GLY K 47
SITE 3 AC2 13 ALA K 49 TYR K 170 HOH K 414 ASP L 126
SITE 4 AC2 13 VAL L 128
SITE 1 AC3 14 HIS H 116 HOH H 412 THR N 1 ARG N 19
SITE 2 AC3 14 THR N 20 THR N 21 THR N 22 LYS N 33
SITE 3 AC3 14 ARG N 45 GLY N 47 ALA N 49 THR N 94
SITE 4 AC3 14 SER N 168 HOH N 351
SITE 1 AC4 14 THR V 1 ARG V 19 SER V 20 THR V 21
SITE 2 AC4 14 CYS V 31 LYS V 33 ALA V 46 GLY V 47
SITE 3 AC4 14 ALA V 49 THR V 52 SER V 129 GLY V 168
SITE 4 AC4 14 ASP W 124 ILE W 126
SITE 1 AC5 11 THR Y 1 ARG Y 19 ALA Y 20 THR Y 21
SITE 2 AC5 11 VAL Y 31 MET Y 45 GLY Y 47 ALA Y 49
SITE 3 AC5 11 SER Y 96 TYR Y 170 ASP Z 126
SITE 1 AC6 14 HIS V 116 THR b 1 ARG b 19 THR b 20
SITE 2 AC6 14 THR b 21 LYS b 33 ARG b 45 GLY b 47
SITE 3 AC6 14 SER b 48 ALA b 49 THR b 52 THR b 94
SITE 4 AC6 14 SER b 168 HOH b 346
CRYST1 134.410 300.780 143.820 90.00 112.75 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 0.007440 0.000000 0.003120 0.00000
SCALE2 0.000000 0.003325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007540 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 -0.999670 -0.003009 0.025512 67.17863 1
MTRIX2 2 -0.001333 -0.985702 -0.168494 -290.05682 1
MTRIX3 2 0.025654 -0.168472 0.985373 -25.34050 1
(ATOM LINES ARE NOT SHOWN.)
END
