HEADER HYDROLASE/HYDROLASE INHIBTIOR 15-NOV-11 3UN8
TITLE YEAST 20S PROTEASOME IN COMPLEX WITH PR-957 (EPOXIDE)
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 INHIBTIOR 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 3UN8 1 REMARK LINK
REVDAT 2 28-MAR-12 3UN8 1 JRNL
REVDAT 1 29-FEB-12 3UN8 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 272564
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 14346
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19258
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 1015
REMARK 3 BIN FREE R VALUE : 0.3560
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 : 36
REMARK 3 SOLVENT ATOMS : 1340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.18000
REMARK 3 B22 (A**2) : -5.66000
REMARK 3 B33 (A**2) : 2.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.79000
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): 0.285
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.971
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50490 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68308 ; 0.832 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6340 ; 3.975 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2264 ;34.602 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8780 ;13.128 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 288 ; 9.097 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7688 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 37978 ; 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): 50490 ; 1.205 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 333 ;22.807 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 50591 ;20.850 ; 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 1338
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1869 -92.5554 45.6575
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.0154
REMARK 3 T33: 0.0402 T12: -0.0069
REMARK 3 T13: 0.0015 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.1665 L22: 0.1379
REMARK 3 L33: 0.0282 L12: -0.0634
REMARK 3 L13: -0.0009 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.0012 S13: 0.0039
REMARK 3 S21: 0.0135 S22: 0.0046 S23: -0.0221
REMARK 3 S31: -0.0099 S32: 0.0056 S33: -0.0029
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 1315
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5604 -88.2149 16.2167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0670 T22: 0.0143
REMARK 3 T33: 0.0380 T12: -0.0047
REMARK 3 T13: 0.0140 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.1556 L22: 0.0374
REMARK 3 L33: 0.1005 L12: 0.0529
REMARK 3 L13: 0.0090 L23: -0.0076
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: -0.0007 S13: 0.0092
REMARK 3 S21: -0.0108 S22: 0.0062 S23: -0.0110
REMARK 3 S31: -0.0083 S32: 0.0198 S33: 0.0053
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 1328
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2607 -87.4769 0.9796
REMARK 3 T TENSOR
REMARK 3 T11: 0.0725 T22: 0.0173
REMARK 3 T33: 0.0353 T12: 0.0000
REMARK 3 T13: 0.0015 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.0519 L22: 0.0914
REMARK 3 L33: 0.1656 L12: 0.0196
REMARK 3 L13: -0.0368 L23: -0.0394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: 0.0105 S13: 0.0167
REMARK 3 S21: -0.0192 S22: 0.0102 S23: 0.0101
REMARK 3 S31: -0.0078 S32: 0.0180 S33: -0.0033
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 1334
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6934 -90.6394 14.4663
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.0118
REMARK 3 T33: 0.0624 T12: 0.0091
REMARK 3 T13: -0.0117 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.0134 L22: 0.0501
REMARK 3 L33: 0.1155 L12: -0.0151
REMARK 3 L13: -0.0066 L23: -0.0368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: -0.0006 S13: 0.0042
REMARK 3 S21: -0.0105 S22: 0.0075 S23: 0.0277
REMARK 3 S31: -0.0006 S32: 0.0092 S33: -0.0119
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 1301
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5914 -94.2568 45.7845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: 0.0169
REMARK 3 T33: 0.0627 T12: 0.0115
REMARK 3 T13: 0.0164 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.1326 L22: 0.0143
REMARK 3 L33: 0.1210 L12: -0.0112
REMARK 3 L13: 0.0472 L23: -0.0194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.0018 S13: -0.0021
REMARK 3 S21: 0.0024 S22: 0.0078 S23: 0.0227
REMARK 3 S31: -0.0134 S32: -0.0171 S33: 0.0010
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 1341
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9043 -95.0580 69.6799
REMARK 3 T TENSOR
REMARK 3 T11: 0.0753 T22: 0.0192
REMARK 3 T33: 0.0250 T12: 0.0051
REMARK 3 T13: 0.0380 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.1406 L22: 0.0238
REMARK 3 L33: 0.0531 L12: 0.0085
REMARK 3 L13: -0.0226 L23: 0.0306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: -0.0035 S13: 0.0156
REMARK 3 S21: 0.0187 S22: -0.0023 S23: 0.0096
REMARK 3 S31: 0.0074 S32: -0.0060 S33: 0.0010
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 1293
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0817 -93.5956 70.8084
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.0102
REMARK 3 T33: 0.0271 T12: -0.0082
REMARK 3 T13: 0.0029 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.0818 L22: 0.0737
REMARK 3 L33: 0.0521 L12: -0.0217
REMARK 3 L13: -0.0190 L23: -0.0304
REMARK 3 S TENSOR
REMARK 3 S11: -0.0020 S12: -0.0133 S13: 0.0057
REMARK 3 S21: 0.0227 S22: 0.0026 S23: -0.0100
REMARK 3 S31: -0.0044 S32: -0.0053 S33: -0.0005
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 RESIDUE RANGE : H 233 H 1308
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6658-130.3729 48.1410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0614 T22: 0.0155
REMARK 3 T33: 0.0486 T12: 0.0008
REMARK 3 T13: -0.0049 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0711 L22: 0.0483
REMARK 3 L33: 0.0216 L12: -0.0115
REMARK 3 L13: -0.0229 L23: 0.0266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: 0.0097 S13: 0.0112
REMARK 3 S21: 0.0186 S22: 0.0024 S23: -0.0436
REMARK 3 S31: 0.0014 S32: -0.0072 S33: -0.0148
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 1342
REMARK 3 ORIGIN FOR THE GROUP (A): 68.3551-127.8053 20.7846
REMARK 3 T TENSOR
REMARK 3 T11: 0.0530 T22: 0.0165
REMARK 3 T33: 0.0462 T12: 0.0014
REMARK 3 T13: 0.0133 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.0225 L22: 0.1721
REMARK 3 L33: 0.1104 L12: -0.0217
REMARK 3 L13: -0.0470 L23: 0.0516
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.0034 S13: 0.0067
REMARK 3 S21: 0.0030 S22: -0.0018 S23: -0.0352
REMARK 3 S31: -0.0054 S32: -0.0005 S33: -0.0106
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 1335
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8197-126.9228 -1.0326
REMARK 3 T TENSOR
REMARK 3 T11: 0.0696 T22: 0.0207
REMARK 3 T33: 0.0229 T12: -0.0007
REMARK 3 T13: 0.0139 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.1685 L22: 0.1886
REMARK 3 L33: 0.0562 L12: -0.0549
REMARK 3 L13: 0.0657 L23: 0.0507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: -0.0037 S13: -0.0100
REMARK 3 S21: -0.0333 S22: -0.0004 S23: 0.0008
REMARK 3 S31: -0.0103 S32: -0.0037 S33: -0.0054
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 1333
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0442-131.1780 2.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0614 T22: 0.0202
REMARK 3 T33: 0.0384 T12: 0.0052
REMARK 3 T13: -0.0168 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0646 L22: 0.1200
REMARK 3 L33: 0.0581 L12: 0.0311
REMARK 3 L13: 0.0199 L23: 0.0035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: 0.0070 S13: 0.0054
REMARK 3 S21: -0.0255 S22: 0.0105 S23: 0.0246
REMARK 3 S31: -0.0114 S32: 0.0062 S33: -0.0116
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 1322
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0204-134.5622 28.6658
REMARK 3 T TENSOR
REMARK 3 T11: 0.0427 T22: 0.0145
REMARK 3 T33: 0.0604 T12: 0.0022
REMARK 3 T13: -0.0048 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0754 L22: 0.0770
REMARK 3 L33: 0.0530 L12: -0.0074
REMARK 3 L13: 0.0006 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: 0.0005 S13: 0.0093
REMARK 3 S21: 0.0021 S22: -0.0074 S23: 0.0303
REMARK 3 S31: 0.0000 S32: 0.0009 S33: -0.0066
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 1332
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9999-137.9394 60.3942
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.0183
REMARK 3 T33: 0.0386 T12: -0.0036
REMARK 3 T13: 0.0228 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0919 L22: 0.1670
REMARK 3 L33: 0.0614 L12: 0.0048
REMARK 3 L13: 0.0314 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: 0.0005 S13: 0.0068
REMARK 3 S21: 0.0411 S22: -0.0116 S23: 0.0288
REMARK 3 S31: -0.0006 S32: 0.0035 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 RESIDUE RANGE : N 197 N 1230
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9225-134.3692 70.6228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: 0.0193
REMARK 3 T33: 0.0062 T12: -0.0014
REMARK 3 T13: 0.0031 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0892 L22: 0.1623
REMARK 3 L33: 0.0572 L12: -0.0073
REMARK 3 L13: -0.0322 L23: -0.0430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: -0.0092 S13: -0.0014
REMARK 3 S21: 0.0362 S22: 0.0081 S23: 0.0015
REMARK 3 S31: -0.0052 S32: 0.0020 S33: -0.0106
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 1323
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0255-206.8113 36.7899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0603 T22: 0.0127
REMARK 3 T33: 0.0521 T12: -0.0102
REMARK 3 T13: -0.0064 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.1707 L22: 0.0866
REMARK 3 L33: 0.0567 L12: -0.0492
REMARK 3 L13: -0.0440 L23: 0.0191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.0017 S13: 0.0016
REMARK 3 S21: 0.0102 S22: 0.0064 S23: 0.0141
REMARK 3 S31: 0.0155 S32: -0.0062 S33: -0.0033
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 1337
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7732-205.9643 6.7948
REMARK 3 T TENSOR
REMARK 3 T11: 0.0660 T22: 0.0096
REMARK 3 T33: 0.0452 T12: -0.0020
REMARK 3 T13: -0.0156 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.1243 L22: 0.0509
REMARK 3 L33: 0.1163 L12: 0.0098
REMARK 3 L13: 0.0521 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: -0.0122 S13: -0.0027
REMARK 3 S21: -0.0049 S22: 0.0062 S23: 0.0127
REMARK 3 S31: -0.0029 S32: -0.0168 S33: 0.0032
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 1324
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8533-204.1465 -9.1597
REMARK 3 T TENSOR
REMARK 3 T11: 0.0826 T22: 0.0157
REMARK 3 T33: 0.0327 T12: 0.0034
REMARK 3 T13: -0.0060 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.0318 L22: 0.0934
REMARK 3 L33: 0.1263 L12: -0.0049
REMARK 3 L13: 0.0293 L23: -0.0952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: 0.0072 S13: -0.0117
REMARK 3 S21: -0.0337 S22: 0.0126 S23: 0.0191
REMARK 3 S31: 0.0250 S32: -0.0083 S33: -0.0194
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 273 R 1302
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7101-203.2194 3.9678
REMARK 3 T TENSOR
REMARK 3 T11: 0.0554 T22: 0.0192
REMARK 3 T33: 0.0416 T12: 0.0155
REMARK 3 T13: 0.0253 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.0436 L22: 0.1000
REMARK 3 L33: 0.1162 L12: -0.0594
REMARK 3 L13: -0.0069 L23: -0.0222
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: 0.0040 S13: 0.0162
REMARK 3 S21: -0.0214 S22: -0.0035 S23: -0.0228
REMARK 3 S31: 0.0185 S32: -0.0036 S33: -0.0096
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 1319
REMARK 3 ORIGIN FOR THE GROUP (A): 71.8052-204.8796 35.2086
REMARK 3 T TENSOR
REMARK 3 T11: 0.0503 T22: 0.0127
REMARK 3 T33: 0.0642 T12: 0.0154
REMARK 3 T13: -0.0056 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.1246 L22: 0.0240
REMARK 3 L33: 0.0665 L12: 0.0313
REMARK 3 L13: -0.0531 L23: -0.0254
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: 0.0170 S13: -0.0181
REMARK 3 S21: 0.0108 S22: 0.0028 S23: -0.0207
REMARK 3 S31: 0.0111 S32: 0.0100 S33: -0.0119
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 1340
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8676-208.2136 59.3203
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.0067
REMARK 3 T33: 0.0453 T12: 0.0060
REMARK 3 T13: -0.0291 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.1036 L22: 0.0339
REMARK 3 L33: 0.0891 L12: 0.0275
REMARK 3 L13: 0.0575 L23: -0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: -0.0069 S13: -0.0334
REMARK 3 S21: 0.0131 S22: -0.0052 S23: -0.0165
REMARK 3 S31: 0.0071 S32: -0.0019 S33: -0.0166
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 1330
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7998-210.1578 61.0355
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0110
REMARK 3 T33: 0.0391 T12: -0.0045
REMARK 3 T13: -0.0074 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.0470 L22: 0.0323
REMARK 3 L33: 0.0396 L12: -0.0370
REMARK 3 L13: 0.0195 L23: -0.0165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: -0.0062 S13: -0.0090
REMARK 3 S21: 0.0065 S22: 0.0081 S23: 0.0175
REMARK 3 S31: -0.0077 S32: 0.0116 S33: -0.0038
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 RESIDUE RANGE : V 233 V 1327
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6653-169.9496 45.7186
REMARK 3 T TENSOR
REMARK 3 T11: 0.0557 T22: 0.0121
REMARK 3 T33: 0.0514 T12: -0.0027
REMARK 3 T13: -0.0006 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0796 L22: 0.0331
REMARK 3 L33: 0.0171 L12: -0.0226
REMARK 3 L13: 0.0329 L23: -0.0136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.0006 S13: -0.0047
REMARK 3 S21: 0.0109 S22: 0.0009 S23: 0.0356
REMARK 3 S31: 0.0127 S32: -0.0003 S33: -0.0099
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 1336
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3076-167.8074 18.3161
REMARK 3 T TENSOR
REMARK 3 T11: 0.0585 T22: 0.0118
REMARK 3 T33: 0.0548 T12: 0.0020
REMARK 3 T13: -0.0123 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.0164 L22: 0.2017
REMARK 3 L33: 0.0799 L12: -0.0222
REMARK 3 L13: 0.0356 L23: -0.0476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: 0.0013 S13: -0.0080
REMARK 3 S21: 0.0085 S22: 0.0047 S23: 0.0361
REMARK 3 S31: -0.0029 S32: 0.0048 S33: -0.0060
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 1265
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2887-164.8782 -4.0089
REMARK 3 T TENSOR
REMARK 3 T11: 0.0733 T22: 0.0176
REMARK 3 T33: 0.0288 T12: 0.0014
REMARK 3 T13: -0.0153 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.1073 L22: 0.1408
REMARK 3 L33: 0.0468 L12: -0.0278
REMARK 3 L13: -0.0573 L23: -0.0307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: -0.0028 S13: -0.0021
REMARK 3 S21: -0.0273 S22: -0.0002 S23: 0.0070
REMARK 3 S31: 0.0034 S32: 0.0022 S33: -0.0057
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 1321
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1568-161.2108 -0.7632
REMARK 3 T TENSOR
REMARK 3 T11: 0.0556 T22: 0.0230
REMARK 3 T33: 0.0250 T12: 0.0079
REMARK 3 T13: 0.0284 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.1058 L22: 0.0973
REMARK 3 L33: 0.0110 L12: 0.0385
REMARK 3 L13: -0.0052 L23: -0.0157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: 0.0108 S13: -0.0072
REMARK 3 S21: -0.0270 S22: 0.0090 S23: -0.0154
REMARK 3 S31: 0.0015 S32: 0.0046 S33: -0.0106
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 1311
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8652-162.3040 25.1563
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0160
REMARK 3 T33: 0.0573 T12: 0.0050
REMARK 3 T13: 0.0081 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0577 L22: 0.0731
REMARK 3 L33: 0.1060 L12: -0.0192
REMARK 3 L13: -0.0215 L23: 0.0025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: 0.0075 S13: -0.0120
REMARK 3 S21: 0.0042 S22: -0.0018 S23: -0.0282
REMARK 3 S31: -0.0030 S32: 0.0035 S33: -0.0073
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 1307
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6304-164.3966 57.3249
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: 0.0119
REMARK 3 T33: 0.0426 T12: -0.0030
REMARK 3 T13: -0.0153 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.0842 L22: 0.1169
REMARK 3 L33: 0.0682 L12: -0.0189
REMARK 3 L13: 0.0207 L23: 0.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.0005 S13: -0.0135
REMARK 3 S21: 0.0337 S22: -0.0043 S23: -0.0256
REMARK 3 S31: 0.0059 S32: -0.0050 S33: -0.0135
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 RESIDUE RANGE : b 197 b 1250
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9576-169.7853 67.7273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0157
REMARK 3 T33: 0.0108 T12: -0.0035
REMARK 3 T13: 0.0049 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.1559 L22: 0.1465
REMARK 3 L33: 0.1144 L12: 0.0075
REMARK 3 L13: 0.0350 L23: 0.0844
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: -0.0062 S13: -0.0023
REMARK 3 S21: 0.0202 S22: 0.0107 S23: 0.0027
REMARK 3 S31: 0.0112 S32: -0.0042 S33: -0.0210
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 3UN8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068965.
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 : 286910
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.59600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 (%): 66.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
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 150.21000
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: 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 2 124.55 69.42
REMARK 500 TYR A 97 -61.09 -138.49
REMARK 500 LYS A 166 -70.51 -59.57
REMARK 500 ARG B 8 78.04 59.65
REMARK 500 THR B 10 51.84 -113.07
REMARK 500 VAL B 51 99.24 58.21
REMARK 500 ARG B 142 -62.26 -92.99
REMARK 500 ASP B 221 -53.34 -149.01
REMARK 500 LEU C 52 24.81 -168.19
REMARK 500 PRO C 183 103.77 -51.14
REMARK 500 GLN C 202 76.98 64.47
REMARK 500 THR C 203 94.06 58.31
REMARK 500 ARG D 45 77.24 54.94
REMARK 500 GLU D 122 -143.55 -147.86
REMARK 500 GLU D 123 65.66 -115.82
REMARK 500 SER E 39 -143.20 -121.97
REMARK 500 ASP E 137 -151.22 -119.69
REMARK 500 ARG E 201 -43.75 -151.64
REMARK 500 ASP F 67 -122.92 57.79
REMARK 500 LYS F 100 -51.79 69.70
REMARK 500 ASP F 138 -148.17 -123.26
REMARK 500 ASP G 40 26.65 -142.91
REMARK 500 LYS G 165 44.26 -105.33
REMARK 500 LYS G 181 -17.82 71.58
REMARK 500 GLN G 242 -43.83 -130.72
REMARK 500 SER H 171 -121.33 63.84
REMARK 500 GLN I 31 -115.42 60.44
REMARK 500 ARG I 97 55.66 -107.27
REMARK 500 ASP I 134 -78.45 -91.06
REMARK 500 VAL J 9 -153.34 -97.41
REMARK 500 SER J 31 31.78 -147.61
REMARK 500 LYS J 34 46.61 -86.58
REMARK 500 PRO J 40 -34.49 -38.79
REMARK 500 ASP J 185 -157.15 -134.36
REMARK 500 ASP J 194 69.46 -111.57
REMARK 500 ASP K 147 34.37 -85.92
REMARK 500 ASP L 32 -99.61 54.87
REMARK 500 LYS L 100 54.70 -110.24
REMARK 500 PHE L 103 70.73 -150.66
REMARK 500 ASP L 200 -67.37 67.68
REMARK 500 ILE M 5 -66.79 -104.65
REMARK 500 THR M 9 -156.10 -79.19
REMARK 500 TYR M 16 -167.48 -112.83
REMARK 500 ASN M 26 30.99 -95.81
REMARK 500 ALA M 83 -109.38 -129.14
REMARK 500 GLU M 85 33.46 -99.05
REMARK 500 LYS N 107 -122.23 62.22
REMARK 500 THR O 2 125.71 70.88
REMARK 500 TYR O 97 -61.61 -135.25
REMARK 500 ARG P 8 77.66 60.16
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE LIGAND 049 FOR CHAIN Y AND K PRESENTS A HEMIKETAL-FORMATION
REMARK 600 WITH THR1. THE EPOXIDE-RING IS INTACT
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 049 K 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 049 Y 213
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: 3UN4 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
DBREF 3UN8 A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 3UN8 B 0 257 UNP P23638 PSA4_YEAST 1 258
DBREF 3UN8 C -1 252 UNP P40303 PSA7_YEAST 1 254
DBREF 3UN8 D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 3UN8 E 0 233 UNP P40302 PSA1_YEAST 1 234
DBREF 3UN8 F -3 284 UNP P21242 PSA3_YEAST 1 288
DBREF 3UN8 G -8 243 UNP P21243 PSA6_YEAST 1 252
DBREF 3UN8 H 1 232 UNP P25043 PSB7_YEAST 30 261
DBREF 3UN8 I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 3UN8 J 1 198 UNP P22141 PSB2_YEAST 1 198
DBREF 3UN8 K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 3UN8 L 1 222 UNP P23724 PSB1_YEAST 20 241
DBREF 3UN8 M 1 233 UNP P30657 PSB4_YEAST 34 266
DBREF 3UN8 N 1 196 UNP P38624 PSB6_YEAST 20 215
DBREF 3UN8 O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 3UN8 P 0 257 UNP P23638 PSA4_YEAST 1 258
DBREF 3UN8 Q -1 252 UNP P40303 PSA7_YEAST 1 254
DBREF 3UN8 R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 3UN8 S 0 233 UNP P40302 PSA1_YEAST 1 234
DBREF 3UN8 T -3 284 UNP P21242 PSA3_YEAST 1 288
DBREF 3UN8 U -8 243 UNP P21243 PSA6_YEAST 1 252
DBREF 3UN8 V 1 232 UNP P25043 PSB7_YEAST 30 261
DBREF 3UN8 W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 3UN8 X 1 198 UNP P22141 PSB2_YEAST 1 198
DBREF 3UN8 Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 3UN8 Z 1 222 UNP P23724 PSB1_YEAST 20 241
DBREF 3UN8 a 1 233 UNP P30657 PSB4_YEAST 34 266
DBREF 3UN8 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 049 K 213 18
HET 049 Y 213 18
HETNAM 049 2-(ACETYLAMINO)-4,5-ANHYDRO-1,2-DIDEOXY-4-METHYL-1-
HETNAM 2 049 PHENYL-D-XYLITOL
FORMUL 29 049 2(C14 H19 N O3)
FORMUL 31 HOH *1340(H2 O)
HELIX 1 1 LEU A 18 GLY A 31 1 14
HELIX 2 2 MET A 78 SER A 96 1 19
HELIX 3 3 TYR A 97 GLY A 102 1 6
HELIX 4 4 PRO A 106 SER A 124 1 19
HELIX 5 5 GLY A 167 TRP A 179 1 13
HELIX 6 6 GLU A 184 GLU A 198 1 15
HELIX 7 7 ASN A 218 LEU A 222 5 5
HELIX 8 8 THR A 239 GLU A 248 1 10
HELIX 9 9 SER B 2 ASP B 6 5 5
HELIX 10 10 LEU B 18 SER B 29 1 12
HELIX 11 11 LEU B 79 ASN B 102 1 24
HELIX 12 12 PRO B 106 HIS B 124 1 19
HELIX 13 13 ASN B 167 TYR B 179 1 13
HELIX 14 14 LYS B 184 THR B 200 1 17
HELIX 15 15 THR B 206 ASP B 208 5 3
HELIX 16 16 LYS B 230 THR B 241 1 12
HELIX 17 17 ILE C 15 GLY C 28 1 14
HELIX 18 18 LEU C 76 LEU C 98 1 23
HELIX 19 19 THR C 103 TYR C 118 1 16
HELIX 20 20 ASN C 165 LYS C 175 1 11
HELIX 21 21 THR C 185 GLN C 202 1 18
HELIX 22 22 SER C 223 GLU C 240 1 18
HELIX 23 23 LEU D 13 LYS D 24 1 12
HELIX 24 24 GLU D 52 ILE D 56 5 5
HELIX 25 25 ASP D 76 ASP D 96 1 21
HELIX 26 26 ASN D 100 ASP D 110 1 11
HELIX 27 27 GLY D 167 TRP D 179 1 13
HELIX 28 28 THR D 184 MET D 200 1 17
HELIX 29 29 ASP D 224 GLU D 242 1 19
HELIX 30 30 PHE E 1 TYR E 5 5 5
HELIX 31 31 LEU E 18 GLY E 31 1 14
HELIX 32 32 LEU E 76 PHE E 98 1 23
HELIX 33 33 ALA E 103 SER E 121 1 19
HELIX 34 34 ARG E 163 THR E 174 1 12
HELIX 35 35 THR E 174 ILE E 179 1 6
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 GLY F 30 1 14
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 GLY F 229 ILE F 243 1 15
HELIX 46 46 ALA G 1 HIS G 6 5 6
HELIX 47 47 LEU G 16 ALA G 25 1 10
HELIX 48 48 THR G 26 GLN G 28 5 3
HELIX 49 49 PRO G 77 GLY G 100 1 24
HELIX 50 50 PRO G 104 ARG G 122 1 19
HELIX 51 51 LYS G 165 LYS G 181 1 17
HELIX 52 52 SER G 189 GLY G 206 1 18
HELIX 53 53 SER G 228 GLU G 241 1 14
HELIX 54 54 THR H 48 SER H 71 1 24
HELIX 55 55 ARG H 75 TYR H 90 1 16
HELIX 56 56 GLY H 130 TRP H 142 1 13
HELIX 57 57 THR H 147 ASP H 166 1 20
HELIX 58 58 LEU I 55 GLU I 78 1 24
HELIX 59 59 GLU I 82 GLU I 96 1 15
HELIX 60 60 ALA I 141 TYR I 153 1 13
HELIX 61 61 GLU I 158 ASP I 175 1 18
HELIX 62 62 GLY J 51 ASP J 72 1 22
HELIX 63 63 SER J 76 ILE J 92 1 17
HELIX 64 64 TYR J 135 TYR J 148 1 14
HELIX 65 65 THR J 153 MET J 172 1 20
HELIX 66 66 GLY K 48 LYS K 71 1 24
HELIX 67 67 SER K 75 TYR K 90 1 16
HELIX 68 68 GLY K 132 TYR K 144 1 13
HELIX 69 69 SER K 149 ASP K 168 1 20
HELIX 70 70 VAL K 193 GLY K 205 1 13
HELIX 71 71 PHE L 57 HIS L 79 1 23
HELIX 72 72 SER L 85 GLY L 99 1 15
HELIX 73 73 ALA L 142 VAL L 154 1 13
HELIX 74 74 SER L 176 HIS L 195 1 20
HELIX 75 75 ILE M 57 TYR M 76 1 20
HELIX 76 76 GLU M 88 LYS M 106 1 19
HELIX 77 77 GLY M 145 ARG M 156 1 12
HELIX 78 78 ARG M 161 ILE M 165 5 5
HELIX 79 79 THR M 169 ASP M 188 1 20
HELIX 80 80 TRP M 219 LYS M 223 5 5
HELIX 81 81 SER N 48 GLY N 71 1 24
HELIX 82 82 SER N 74 ASN N 89 1 16
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 78 SER O 96 1 19
HELIX 89 89 TYR O 97 GLY O 102 1 6
HELIX 90 90 PRO O 106 SER O 124 1 19
HELIX 91 91 GLY O 167 TRP O 179 1 13
HELIX 92 92 GLU O 184 GLU O 198 1 15
HELIX 93 93 THR O 239 GLU O 248 1 10
HELIX 94 94 SER P 2 ASP P 6 5 5
HELIX 95 95 LEU P 18 SER P 29 1 12
HELIX 96 96 LEU P 79 ASN P 102 1 24
HELIX 97 97 PRO P 106 HIS P 124 1 19
HELIX 98 98 ASN P 167 TYR P 179 1 13
HELIX 99 99 LYS P 184 THR P 200 1 17
HELIX 100 100 THR P 206 ASP P 208 5 3
HELIX 101 101 LYS P 230 THR P 241 1 12
HELIX 102 102 ILE Q 15 GLY Q 28 1 14
HELIX 103 103 LEU Q 76 LEU Q 98 1 23
HELIX 104 104 THR Q 103 TYR Q 118 1 16
HELIX 105 105 ASN Q 165 LYS Q 175 1 11
HELIX 106 106 THR Q 185 GLN Q 202 1 18
HELIX 107 107 SER Q 223 GLU Q 240 1 18
HELIX 108 108 LEU R 13 LYS R 24 1 12
HELIX 109 109 GLU R 52 ILE R 56 5 5
HELIX 110 110 ASP R 76 ASP R 96 1 21
HELIX 111 111 ASN R 100 ASP R 110 1 11
HELIX 112 112 GLY R 167 TRP R 179 1 13
HELIX 113 113 THR R 184 MET R 200 1 17
HELIX 114 114 ASP R 224 GLU R 242 1 19
HELIX 115 115 PHE S 1 TYR S 5 5 5
HELIX 116 116 LEU S 18 GLY S 31 1 14
HELIX 117 117 LEU S 76 PHE S 98 1 23
HELIX 118 118 ALA S 103 SER S 121 1 19
HELIX 119 119 ARG S 163 THR S 174 1 12
HELIX 120 120 THR S 174 ILE S 179 1 6
HELIX 121 121 ASN S 184 SER S 197 1 14
HELIX 122 122 GLN S 198 LEU S 200 5 3
HELIX 123 123 GLU S 227 ILE S 233 5 7
HELIX 124 124 ASN T 17 GLY T 30 1 14
HELIX 125 125 LEU T 77 LYS T 100 1 24
HELIX 126 126 PRO T 104 HIS T 119 1 16
HELIX 127 127 GLY T 164 HIS T 179 1 16
HELIX 128 128 SER T 184 HIS T 200 1 17
HELIX 129 129 GLU T 201 ASN T 203 5 3
HELIX 130 130 GLY T 229 ILE T 243 1 15
HELIX 131 131 ALA U 1 HIS U 6 5 6
HELIX 132 132 LEU U 16 ALA U 25 1 10
HELIX 133 133 THR U 26 GLN U 28 5 3
HELIX 134 134 PRO U 77 GLY U 100 1 24
HELIX 135 135 PRO U 104 ARG U 122 1 19
HELIX 136 136 LYS U 165 LYS U 181 1 17
HELIX 137 137 SER U 189 GLY U 206 1 18
HELIX 138 138 SER U 228 GLU U 241 1 14
HELIX 139 139 THR V 48 SER V 71 1 24
HELIX 140 140 ARG V 75 TYR V 90 1 16
HELIX 141 141 GLY V 130 TRP V 142 1 13
HELIX 142 142 THR V 147 ASP V 166 1 20
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 VAL Z 154 1 13
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 GLY a 145 ARG a 156 1 12
HELIX 163 163 ARG a 161 ILE a 165 5 5
HELIX 164 164 THR a 169 ASP a 188 1 20
HELIX 165 165 TRP a 219 LYS a 223 5 5
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 GLY b 128 PHE b 133 5 6
HELIX 169 169 ILE b 134 PHE b 142 1 9
HELIX 170 170 SER b 147 ASP b 166 1 20
HELIX 171 171 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 6 ALA A 56 MET A 57 0
SHEET 2 B 6 TYR G 154 TYR G 157 -1 O GLY G 156 N MET A 57
SHEET 3 B 6 GLY G 142 THR G 148 -1 N ILE G 145 O TYR G 157
SHEET 4 B 6 ILE G 131 ASP G 138 -1 N PHE G 134 O TYR G 146
SHEET 5 B 6 GLY G 71 ASN G 75 -1 N GLY G 71 O VAL G 135
SHEET 6 B 6 ILE G 63 CYS G 65 -1 N PHE G 64 O MET G 72
SHEET 1 C 5 SER A 65 THR A 68 0
SHEET 2 C 5 ILE A 71 GLY A 77 -1 O ILE A 71 N LEU A 67
SHEET 3 C 5 VAL A 132 ASP A 140 -1 O LEU A 135 N VAL A 74
SHEET 4 C 5 GLY A 144 VAL A 150 -1 O VAL A 150 N LEU A 134
SHEET 5 C 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 D 6 TYR A 224 THR A 225 0
SHEET 2 D 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 D 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 D 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 D 6 THR H 2 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 D 6 TYR H 124 GLY H 128 -1 O LEU H 127 N ILE H 3
SHEET 1 E 5 ALA B 161 VAL B 164 0
SHEET 2 E 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 E 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 E 5 LEU B 210 LYS B 217 -1 O ALA B 213 N LEU B 45
SHEET 5 E 5 VAL B 224 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 F 5 LEU B 65 LYS B 67 0
SHEET 2 F 5 ALA B 73 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 F 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 F 5 GLY B 144 SER B 150 -1 O GLN B 146 N GLY B 138
SHEET 5 F 5 TYR B 156 GLY B 158 -1 O THR B 157 N THR B 149
SHEET 1 G 5 ALA C 159 ILE C 162 0
SHEET 2 G 5 ALA C 31 LYS C 35 -1 N ALA C 31 O ILE C 162
SHEET 3 G 5 VAL C 40 GLU C 45 -1 O GLY C 43 N VAL C 32
SHEET 4 G 5 ILE C 208 LYS C 214 -1 O THR C 211 N LEU C 42
SHEET 5 G 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 H 5 SER C 63 LYS C 64 0
SHEET 2 H 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 H 5 VAL C 129 GLY C 135 -1 O LEU C 132 N SER C 72
SHEET 4 H 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 H 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 I 5 ALA D 161 ILE D 164 0
SHEET 2 I 5 ALA D 29 ALA D 33 -1 N ALA D 29 O ILE D 164
SHEET 3 I 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 I 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 I 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 J 5 ILE D 59 ASP D 63 0
SHEET 2 J 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 J 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 J 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 J 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 K 5 GLY E 157 ILE E 160 0
SHEET 2 K 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 K 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 K 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 K 5 THR E 222 ASP E 225 -1 O TYR E 224 N ILE E 212
SHEET 1 L 5 ILE E 62 LYS E 64 0
SHEET 2 L 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 L 5 VAL E 129 ASP E 137 -1 O GLY E 130 N ALA E 74
SHEET 4 L 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 L 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 M 5 GLY F 158 THR F 161 0
SHEET 2 M 5 SER F 33 LYS F 37 -1 N SER F 33 O THR F 161
SHEET 3 M 5 GLY F 41 ILE F 50 -1 O VAL F 43 N ILE F 36
SHEET 4 M 5 ASP F 207 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 M 5 LYS F 225 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 N 5 GLN F 64 VAL F 66 0
SHEET 2 N 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 N 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 N 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 N 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 O 5 ALA G 159 THR G 162 0
SHEET 2 O 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 O 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 O 5 LEU G 214 THR G 220 -1 O ALA G 219 N THR G 42
SHEET 5 O 5 LYS G 223 THR G 226 -1 O LYS G 223 N THR G 220
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 ALA H 101 N TRP H 42
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 VAL H 218 0
SHEET 2 R 6 VAL I 194 LEU I 199 -1 O LYS I 196 N SER H 216
SHEET 3 R 6 ALA I 184 ILE I 189 -1 N VAL I 186 O ARG I 197
SHEET 4 R 6 VAL I 20 ASP I 25 -1 N ILE I 22 O TYR I 187
SHEET 5 R 6 ILE I 10 THR I 15 -1 N MET I 14 O ALA I 21
SHEET 6 R 6 PHE I 135 GLY I 139 -1 O ILE I 136 N ALA I 13
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 4 ILE I 42 TYR I 45 0
SHEET 2 T 4 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 T 4 VAL I 104 ILE I 111 -1 O VAL I 107 N GLY I 51
SHEET 4 T 4 PRO I 118 GLY I 122 -1 O PHE I 119 N GLY I 110
SHEET 1 U 5 TYR J 130 ALA J 132 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 ILE J 14 N ILE J 7
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 VAL J 192 N VAL J 181
SHEET 1 V 2 VAL J 21 ARG J 23 0
SHEET 2 V 2 SER J 26 LYS J 29 -1 O LYS J 29 N VAL J 21
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 GLU J 115 N GLY J 106
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 GLY K 130 0
SHEET 2 X 5 THR K 2 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 191 N VAL K 175
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 GLU K 36 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 VAL L 207 -1 O VAL L 207 N ALA L 21
SHEET 5 AA 5 VAL L 212 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 MET L 52 N PHE L 44
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 ALA L 121 N GLY L 113
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 VAL M 130 N ILE M 114
SHEET 7 AE 7 THR M 136 SER M 138 -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 ILE M 21 N MET M 14
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 THR N 7 -1 N ILE N 3 O ALA N 127
SHEET 3 AG 5 VAL N 12 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AG 5 ILE N 173 LEU N 178 -1 O ARG N 174 N ALA N 16
SHEET 5 AG 5 VAL N 183 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 TYR N 25 N THR N 22
SHEET 1 AI 5 LEU N 34 HIS N 38 0
SHEET 2 AI 5 ILE N 41 GLY N 47 -1 O ILE N 41 N HIS N 38
SHEET 3 AI 5 ALA N 95 ASP N 103 -1 O GLY N 96 N SER N 46
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 6 ALA O 56 MET O 57 0
SHEET 2 AK 6 TYR U 154 TYR U 157 -1 O GLY U 156 N MET O 57
SHEET 3 AK 6 GLY U 142 THR U 148 -1 N ILE U 145 O TYR U 157
SHEET 4 AK 6 ILE U 131 ASP U 138 -1 N PHE U 134 O TYR U 146
SHEET 5 AK 6 GLY U 71 ASN U 75 -1 N GLY U 71 O VAL U 135
SHEET 6 AK 6 ILE U 63 CYS U 65 -1 N PHE U 64 O MET U 72
SHEET 1 AL 5 SER O 65 THR O 68 0
SHEET 2 AL 5 ILE O 71 GLY O 77 -1 O ILE O 71 N LEU O 67
SHEET 3 AL 5 VAL O 132 ASP O 140 -1 O LEU O 135 N VAL O 74
SHEET 4 AL 5 GLY O 144 VAL O 150 -1 O VAL O 150 N LEU O 134
SHEET 5 AL 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AM 6 TYR O 224 THR O 225 0
SHEET 2 AM 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AM 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AM 6 GLY V 11 ASP V 17 -1 N ALA V 16 O ASP V 174
SHEET 5 AM 6 THR V 2 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AM 6 TYR V 124 GLY V 128 -1 O LEU V 127 N ILE V 3
SHEET 1 AN 5 ALA P 161 VAL P 164 0
SHEET 2 AN 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AN 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AN 5 LEU P 210 LYS P 217 -1 O ALA P 213 N LEU P 45
SHEET 5 AN 5 VAL P 224 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AO 5 LEU P 65 LYS P 67 0
SHEET 2 AO 5 ALA P 73 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AO 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AO 5 GLY P 144 SER P 150 -1 O GLN P 146 N GLY P 138
SHEET 5 AO 5 TYR P 156 GLY P 158 -1 O THR P 157 N THR P 149
SHEET 1 AP 5 ALA Q 159 ILE Q 162 0
SHEET 2 AP 5 ALA Q 31 LYS Q 35 -1 N ALA Q 31 O ILE Q 162
SHEET 3 AP 5 VAL Q 40 GLU Q 45 -1 O GLY Q 43 N VAL Q 32
SHEET 4 AP 5 ILE Q 208 LYS Q 214 -1 O THR Q 211 N LEU Q 42
SHEET 5 AP 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AQ 5 SER Q 63 LYS Q 64 0
SHEET 2 AQ 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AQ 5 VAL Q 129 PHE Q 136 -1 O LEU Q 132 N SER Q 72
SHEET 4 AQ 5 PRO Q 143 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AQ 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AR 5 ALA R 161 ILE R 164 0
SHEET 2 AR 5 ALA R 29 ALA R 33 -1 N ALA R 29 O ILE R 164
SHEET 3 AR 5 VAL R 38 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AR 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AR 5 GLY R 219 ILE R 222 -1 O LYS R 221 N CYS R 213
SHEET 1 AS 5 ILE R 59 ASP R 63 0
SHEET 2 AS 5 ILE R 66 GLY R 72 -1 O ILE R 66 N ASP R 63
SHEET 3 AS 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AS 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AS 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AT 5 GLY S 157 ILE S 160 0
SHEET 2 AT 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AT 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AT 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AT 5 THR S 222 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AU 5 ILE S 62 LYS S 64 0
SHEET 2 AU 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AU 5 VAL S 129 ASP S 137 -1 O ILE S 134 N GLY S 70
SHEET 4 AU 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AU 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AV 5 GLY T 158 THR T 161 0
SHEET 2 AV 5 SER T 33 LYS T 37 -1 N SER T 33 O THR T 161
SHEET 3 AV 5 GLY T 41 ILE T 50 -1 O VAL T 43 N ILE T 36
SHEET 4 AV 5 ASP T 207 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AV 5 LYS T 225 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AW 5 GLN T 64 VAL T 66 0
SHEET 2 AW 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AW 5 VAL T 130 VAL T 137 -1 O ILE T 133 N VAL T 73
SHEET 4 AW 5 ALA T 142 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AW 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AX 5 ALA U 159 THR U 162 0
SHEET 2 AX 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AX 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AX 5 LEU U 214 THR U 220 -1 O ALA U 219 N THR U 42
SHEET 5 AX 5 LYS U 223 THR U 226 -1 O LYS U 223 N THR U 220
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 ALA V 101 N TRP V 42
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 LYS W 196 N SER V 216
SHEET 3 BA 6 ALA W 184 ILE W 189 -1 N VAL W 186 O ARG W 197
SHEET 4 BA 6 VAL W 20 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 ILE W 136 N ALA W 13
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 4 ILE W 42 TYR W 45 0
SHEET 2 BC 4 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 BC 4 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 BC 4 PRO W 118 GLY W 122 -1 O ALA W 121 N VAL W 108
SHEET 1 BD 5 TYR X 130 ALA X 132 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 VAL X 192 N VAL X 181
SHEET 1 BE 2 VAL X 21 THR X 22 0
SHEET 2 BE 2 VAL X 27 LYS X 29 -1 O LEU X 28 N VAL X 21
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 GLY X 105 N LEU X 43
SHEET 4 BF 5 LYS X 113 ILE X 119 -1 O ILE X 119 N VAL X 102
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 GLY Y 130 0
SHEET 2 BG 5 THR Y 2 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O ALA Y 15 N LEU Y 4
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 191 N VAL Y 175
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 GLU Y 36 0
SHEET 2 BI 5 LEU Y 42 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 VAL Z 207 -1 O VAL Z 207 N ALA Z 21
SHEET 5 BJ 5 VAL Z 212 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 34 N THR Z 31
SHEET 1 BL 5 PHE Z 44 GLY Z 47 0
SHEET 2 BL 5 ILE Z 50 GLY Z 56 -1 O MET Z 52 N PHE Z 44
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 ALA Z 121 N GLY Z 113
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 VAL a 130 N ILE a 114
SHEET 7 BN 7 THR a 136 SER a 138 -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 ILE a 21 N MET a 14
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 THR b 7 -1 N ILE b 3 O ALA b 127
SHEET 3 BP 5 VAL b 12 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 BP 5 ILE b 173 LEU b 178 -1 O LEU b 178 N VAL b 12
SHEET 5 BP 5 VAL b 183 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 TYR b 25 N THR b 22
SHEET 1 BR 5 LEU b 34 HIS b 38 0
SHEET 2 BR 5 ILE b 41 GLY b 47 -1 O ILE b 41 N HIS b 38
SHEET 3 BR 5 ALA b 95 ASP b 103 -1 O GLY b 96 N SER b 46
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 LEU b 122 N VAL b 110
LINK OG1 THR K 1 C9 049 K 213 1555 1555 1.68
LINK OG1 THR Y 1 C9 049 Y 213 1555 1555 1.58
SITE 1 AC1 9 THR K 1 ARG K 19 THR K 21 MET K 45
SITE 2 AC1 9 ALA K 46 GLY K 47 ALA K 49 SER K 131
SITE 3 AC1 9 TYR K 170
SITE 1 AC2 8 THR Y 1 ARG Y 19 THR Y 21 VAL Y 31
SITE 2 AC2 8 MET Y 45 GLY Y 47 TYR Y 170 HOH Y1202
CRYST1 135.420 300.420 143.930 90.00 112.83 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 0.007384 0.000000 0.003108 0.00000
SCALE2 0.000000 0.003329 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007538 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 -0.999492 -0.003755 0.031639 67.27201 1
MTRIX2 2 -0.001723 -0.985206 -0.171364 -289.99969 1
MTRIX3 2 0.031815 -0.171332 0.984700 -26.06637 1
(ATOM LINES ARE NOT SHOWN.)
END
