HEADER HYDROLASE/HYDROLASE INHIBITOR 15-JUL-14 4QVL
TITLE YCP IN COMPLEX WITH BORTEZOMIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT Y7, PROTEASOME COMPONENT Y7, PROTEINASE YSCE SUBUNIT 7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT Y13, PROTEASOME COMPONENT Y13, PROTEINASE YSCE SUBUNIT 13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 17 SUBUNIT PRE6, PROTEASOME COMPONENT PRE6, PROTEINASE YSCE SUBUNIT
COMPND 18 PRE6;
COMPND 19 EC: 3.4.25.1;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 22 CHAIN: D, R;
COMPND 23 SYNONYM: MACROPAIN SUBUNIT PUP2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 24 SUBUNIT PUP2, PROTEASOME COMPONENT PUP2, PROTEINASE YSCE SUBUNIT
COMPND 25 PUP2;
COMPND 26 EC: 3.4.25.1;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 29 CHAIN: E, S;
COMPND 30 SYNONYM: MACROPAIN SUBUNIT PRE5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 31 SUBUNIT PRE5, PROTEASOME COMPONENT PRE5, PROTEINASE YSCE SUBUNIT
COMPND 32 PRE5;
COMPND 33 EC: 3.4.25.1;
COMPND 34 MOL_ID: 6;
COMPND 35 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 36 CHAIN: F, T;
COMPND 37 SYNONYM: MACROPAIN SUBUNIT C1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 38 SUBUNIT C1, PROTEASOME COMPONENT C1, PROTEINASE YSCE SUBUNIT 1;
COMPND 39 EC: 3.4.25.1;
COMPND 40 MOL_ID: 7;
COMPND 41 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 42 CHAIN: G, U;
COMPND 43 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, MULTICATALYTIC ENDOPEPTIDASE
COMPND 44 COMPLEX C7, PROTEASOME COMPONENT C7-ALPHA, PROTEASOME COMPONENT Y8,
COMPND 45 PROTEINASE YSCE SUBUNIT 7, SCL1 SUPPRESSOR PROTEIN;
COMPND 46 EC: 3.4.25.1;
COMPND 47 MOL_ID: 8;
COMPND 48 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 49 CHAIN: H, V;
COMPND 50 SYNONYM: MACROPAIN SUBUNIT PUP1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 51 SUBUNIT PUP1, PROTEASOME COMPONENT PUP1, PROTEINASE YSCE SUBUNIT
COMPND 52 PUP1;
COMPND 53 EC: 3.4.25.1;
COMPND 54 MOL_ID: 9;
COMPND 55 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 56 CHAIN: I, W;
COMPND 57 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 58 SUBUNIT PUP3, PROTEASOME COMPONENT PUP3;
COMPND 59 EC: 3.4.25.1;
COMPND 60 MOL_ID: 10;
COMPND 61 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 62 CHAIN: J, X;
COMPND 63 SYNONYM: MACROPAIN SUBUNIT C11, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 64 SUBUNIT C11, PROTEASOME COMPONENT C11, PROTEINASE YSCE SUBUNIT 11;
COMPND 65 EC: 3.4.25.1;
COMPND 66 MOL_ID: 11;
COMPND 67 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 68 CHAIN: K, Y;
COMPND 69 SYNONYM: MACROPAIN SUBUNIT PRE2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 70 SUBUNIT PRE2, PROTEASOME COMPONENT PRE2, PROTEINASE YSCE SUBUNIT
COMPND 71 PRE2;
COMPND 72 EC: 3.4.25.1;
COMPND 73 ENGINEERED: YES;
COMPND 74 MOL_ID: 12;
COMPND 75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 76 CHAIN: L, Z;
COMPND 77 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5, PROTEASOME
COMPND 78 COMPONENT C5;
COMPND 79 EC: 3.4.25.1;
COMPND 80 MOL_ID: 13;
COMPND 81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 82 CHAIN: M, a;
COMPND 83 SYNONYM: MACROPAIN SUBUNIT PRE4, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 84 SUBUNIT PRE4, PROTEASOME COMPONENT PRE4, PROTEINASE YSCE SUBUNIT
COMPND 85 PRE4;
COMPND 86 EC: 3.4.25.1;
COMPND 87 MOL_ID: 14;
COMPND 88 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 89 CHAIN: N, b;
COMPND 90 SYNONYM: MACROPAIN SUBUNIT PRE3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 91 SUBUNIT PRE3, PROTEASOME COMPONENT PRE3, PROTEINASE YSCE SUBUNIT
COMPND 92 PRE3;
COMPND 93 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 GENE: PRE2, DOA3, PRG1, YPR103W, P8283.10;
SOURCE 57 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 58 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 59 MOL_ID: 12;
SOURCE 60 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 61 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 62 ORGANISM_TAXID: 559292;
SOURCE 63 STRAIN: ATCC 204508 / S288C;
SOURCE 64 MOL_ID: 13;
SOURCE 65 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 66 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 67 ORGANISM_TAXID: 559292;
SOURCE 68 STRAIN: ATCC 204508 / S288C;
SOURCE 69 MOL_ID: 14;
SOURCE 70 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 71 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 72 ORGANISM_TAXID: 559292;
SOURCE 73 STRAIN: ATCC 204508 / S288C
KEYWDS CANCER, PROTEASOME, BORTEZOMIB, DRUG RESISTANCE, BINDING ANALYSIS,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,W.HEINEMEYER,M.GROLL
REVDAT 3 20-SEP-23 4QVL 1 REMARK LINK
REVDAT 2 18-FEB-15 4QVL 1 JRNL
REVDAT 1 04-FEB-15 4QVL 0
JRNL AUTH E.M.HUBER,W.HEINEMEYER,M.GROLL
JRNL TITL BORTEZOMIB-RESISTANT MUTANT PROTEASOMES: STRUCTURAL AND
JRNL TITL 2 BIOCHEMICAL EVALUATION WITH CARFILZOMIB AND ONX 0914.
JRNL REF STRUCTURE V. 23 407 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25599643
JRNL DOI 10.1016/J.STR.2014.11.019
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 229137
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12060
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 888
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49366
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.30000
REMARK 3 B22 (A**2) : -6.88000
REMARK 3 B33 (A**2) : 2.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.97000
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): 0.292
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.125
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50454 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48196 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68262 ; 0.874 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES):110966 ; 0.710 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6314 ; 5.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2252 ;34.268 ;24.423
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8752 ;14.124 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;13.941 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7686 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57252 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11322 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25346 ; 2.778 ; 5.668
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25345 ; 2.778 ; 5.668
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31630 ; 3.757 ; 8.487
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31631 ; 3.757 ; 8.487
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25108 ; 2.637 ; 6.064
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25108 ; 2.637 ; 6.064
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36632 ; 3.321 ; 8.941
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54223 ; 4.261 ;44.269
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54188 ; 4.247 ;44.269
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98650 ; 0.909 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 226 ;28.503 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97883 ;17.574 ; 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 301 A 313
REMARK 3 ORIGIN FOR THE GROUP (A): 66.907 -91.890 46.078
REMARK 3 T TENSOR
REMARK 3 T11: 0.1143 T22: 0.0836
REMARK 3 T33: 0.1386 T12: -0.0081
REMARK 3 T13: 0.0002 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.0154 L22: 0.0300
REMARK 3 L33: 0.0019 L12: -0.0153
REMARK 3 L13: -0.0037 L23: 0.0065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: 0.0170 S13: -0.0132
REMARK 3 S21: -0.0041 S22: 0.0046 S23: -0.0119
REMARK 3 S31: -0.0074 S32: -0.0008 S33: 0.0024
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 301 B 314
REMARK 3 ORIGIN FOR THE GROUP (A): 59.520 -87.684 16.497
REMARK 3 T TENSOR
REMARK 3 T11: 0.1067 T22: 0.0882
REMARK 3 T33: 0.1339 T12: -0.0063
REMARK 3 T13: 0.0173 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0029 L22: 0.0060
REMARK 3 L33: 0.0023 L12: 0.0007
REMARK 3 L13: -0.0018 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0077 S12: -0.0088 S13: -0.0107
REMARK 3 S21: -0.0190 S22: -0.0047 S23: 0.0137
REMARK 3 S31: 0.0105 S32: 0.0049 S33: 0.0124
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 240
REMARK 3 RESIDUE RANGE : C 301 C 315
REMARK 3 ORIGIN FOR THE GROUP (A): 32.327 -87.210 1.187
REMARK 3 T TENSOR
REMARK 3 T11: 0.1323 T22: 0.0738
REMARK 3 T33: 0.1333 T12: 0.0053
REMARK 3 T13: 0.0015 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0422 L22: 0.0203
REMARK 3 L33: 0.0012 L12: 0.0276
REMARK 3 L13: 0.0010 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: -0.0137 S13: 0.0030
REMARK 3 S21: -0.0113 S22: 0.0073 S23: 0.0146
REMARK 3 S31: 0.0102 S32: 0.0019 S33: 0.0022
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 301 D 312
REMARK 3 ORIGIN FOR THE GROUP (A): 3.111 -89.895 13.717
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.0551
REMARK 3 T33: 0.1454 T12: 0.0154
REMARK 3 T13: -0.0040 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.0100 L22: 0.0145
REMARK 3 L33: 0.0918 L12: -0.0071
REMARK 3 L13: 0.0139 L23: -0.0238
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: -0.0195 S13: -0.0032
REMARK 3 S21: -0.0133 S22: 0.0057 S23: 0.0280
REMARK 3 S31: -0.0126 S32: 0.0022 S33: -0.0069
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 3 E 233
REMARK 3 RESIDUE RANGE : E 301 E 305
REMARK 3 ORIGIN FOR THE GROUP (A): -3.180 -94.265 45.732
REMARK 3 T TENSOR
REMARK 3 T11: 0.0662 T22: 0.0825
REMARK 3 T33: 0.1308 T12: 0.0197
REMARK 3 T13: 0.0254 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0041
REMARK 3 L33: 0.0281 L12: -0.0033
REMARK 3 L13: 0.0089 L23: -0.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0110 S12: -0.0060 S13: -0.0088
REMARK 3 S21: 0.0102 S22: 0.0080 S23: 0.0183
REMARK 3 S31: 0.0019 S32: -0.0141 S33: 0.0030
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 2 F 244
REMARK 3 RESIDUE RANGE : F 301 F 313
REMARK 3 ORIGIN FOR THE GROUP (A): 15.222 -94.923 69.895
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.0790
REMARK 3 T33: 0.1141 T12: 0.0058
REMARK 3 T13: 0.0424 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.0359 L22: 0.0026
REMARK 3 L33: 0.0014 L12: 0.0072
REMARK 3 L13: 0.0009 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.0063 S13: 0.0006
REMARK 3 S21: 0.0089 S22: -0.0085 S23: 0.0085
REMARK 3 S31: -0.0078 S32: 0.0055 S33: -0.0015
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 RESIDUE RANGE : G 301 G 302
REMARK 3 RESIDUE RANGE : G 401 G 413
REMARK 3 ORIGIN FOR THE GROUP (A): 47.645 -93.264 71.197
REMARK 3 T TENSOR
REMARK 3 T11: 0.1365 T22: 0.0689
REMARK 3 T33: 0.1248 T12: -0.0036
REMARK 3 T13: 0.0050 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0238 L22: 0.0266
REMARK 3 L33: 0.0335 L12: 0.0205
REMARK 3 L13: 0.0198 L23: 0.0272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: 0.0224 S13: -0.0023
REMARK 3 S21: 0.0212 S22: -0.0074 S23: -0.0085
REMARK 3 S31: 0.0037 S32: -0.0074 S33: -0.0001
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 226
REMARK 3 RESIDUE RANGE : H 301 H 301
REMARK 3 RESIDUE RANGE : H 401 H 413
REMARK 3 ORIGIN FOR THE GROUP (A): 67.603 -129.352 47.519
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.0798
REMARK 3 T33: 0.1335 T12: -0.0023
REMARK 3 T13: 0.0019 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.0015 L22: 0.0213
REMARK 3 L33: 0.0040 L12: 0.0011
REMARK 3 L13: -0.0024 L23: -0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: 0.0072 S13: 0.0052
REMARK 3 S21: 0.0354 S22: -0.0009 S23: -0.0309
REMARK 3 S31: -0.0107 S32: -0.0130 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 RESIDUE RANGE : I 301 I 301
REMARK 3 RESIDUE RANGE : I 401 I 410
REMARK 3 ORIGIN FOR THE GROUP (A): 68.237 -127.240 20.984
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.0838
REMARK 3 T33: 0.1350 T12: -0.0060
REMARK 3 T13: 0.0194 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0593
REMARK 3 L33: 0.0093 L12: -0.0184
REMARK 3 L13: 0.0023 L23: -0.0162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.0042 S13: -0.0006
REMARK 3 S21: 0.0091 S22: -0.0099 S23: -0.0162
REMARK 3 S31: -0.0191 S32: -0.0097 S33: 0.0035
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 RESIDUE RANGE : J 201 J 201
REMARK 3 RESIDUE RANGE : J 301 J 313
REMARK 3 ORIGIN FOR THE GROUP (A): 44.730 -126.335 -0.539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.0773
REMARK 3 T33: 0.1083 T12: 0.0012
REMARK 3 T13: 0.0255 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0230 L22: 0.0447
REMARK 3 L33: 0.0029 L12: 0.0257
REMARK 3 L13: -0.0058 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0170 S13: 0.0258
REMARK 3 S21: -0.0213 S22: -0.0063 S23: 0.0110
REMARK 3 S31: 0.0010 S32: 0.0119 S33: -0.0055
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 301 K 302
REMARK 3 RESIDUE RANGE : K 401 K 409
REMARK 3 ORIGIN FOR THE GROUP (A): 10.929 -130.631 2.510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1079 T22: 0.0687
REMARK 3 T33: 0.1285 T12: 0.0055
REMARK 3 T13: -0.0159 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0035 L22: 0.0424
REMARK 3 L33: 0.0062 L12: 0.0080
REMARK 3 L13: -0.0001 L23: 0.0033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: 0.0014 S13: 0.0184
REMARK 3 S21: -0.0095 S22: 0.0023 S23: 0.0193
REMARK 3 S31: -0.0104 S32: 0.0178 S33: -0.0016
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 301 L 325
REMARK 3 ORIGIN FOR THE GROUP (A): -4.508 -134.130 28.632
REMARK 3 T TENSOR
REMARK 3 T11: 0.0881 T22: 0.0797
REMARK 3 T33: 0.1508 T12: 0.0101
REMARK 3 T13: 0.0045 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.0035 L22: 0.0023
REMARK 3 L33: 0.0057 L12: 0.0007
REMARK 3 L13: -0.0032 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0110 S13: 0.0157
REMARK 3 S21: 0.0134 S22: 0.0038 S23: 0.0063
REMARK 3 S31: -0.0163 S32: 0.0117 S33: -0.0067
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 301 M 317
REMARK 3 ORIGIN FOR THE GROUP (A): 7.866 -137.716 60.453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1116 T22: 0.0888
REMARK 3 T33: 0.1347 T12: 0.0020
REMARK 3 T13: 0.0175 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0039 L22: 0.0965
REMARK 3 L33: 0.0010 L12: -0.0147
REMARK 3 L13: 0.0009 L23: -0.0074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.0017 S13: 0.0060
REMARK 3 S21: 0.0169 S22: -0.0082 S23: 0.0144
REMARK 3 S31: -0.0011 S32: 0.0066 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 RESIDUE RANGE : N 201 N 203
REMARK 3 RESIDUE RANGE : N 301 N 316
REMARK 3 ORIGIN FOR THE GROUP (A): 39.859 -133.942 70.729
REMARK 3 T TENSOR
REMARK 3 T11: 0.1316 T22: 0.0863
REMARK 3 T33: 0.1181 T12: -0.0026
REMARK 3 T13: 0.0015 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0543 L22: 0.0926
REMARK 3 L33: 0.0162 L12: -0.0360
REMARK 3 L13: -0.0252 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.0050 S13: -0.0004
REMARK 3 S21: 0.0225 S22: -0.0126 S23: 0.0064
REMARK 3 S31: 0.0020 S32: -0.0043 S33: 0.0042
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 301 O 304
REMARK 3 ORIGIN FOR THE GROUP (A): 1.785 -206.284 36.738
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.0823
REMARK 3 T33: 0.1416 T12: -0.0161
REMARK 3 T13: -0.0126 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0285 L22: 0.0603
REMARK 3 L33: 0.0179 L12: 0.0211
REMARK 3 L13: -0.0036 L23: 0.0171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0202 S13: 0.0073
REMARK 3 S21: -0.0041 S22: 0.0007 S23: -0.0063
REMARK 3 S31: 0.0238 S32: -0.0025 S33: -0.0003
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 301 P 311
REMARK 3 ORIGIN FOR THE GROUP (A): 8.384 -205.145 6.680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1149 T22: 0.0737
REMARK 3 T33: 0.1473 T12: -0.0019
REMARK 3 T13: -0.0176 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.0037 L22: 0.0025
REMARK 3 L33: 0.0233 L12: -0.0002
REMARK 3 L13: 0.0067 L23: -0.0019
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.0081 S13: 0.0095
REMARK 3 S21: -0.0083 S22: 0.0018 S23: -0.0148
REMARK 3 S31: -0.0098 S32: -0.0105 S33: 0.0138
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 240
REMARK 3 RESIDUE RANGE : Q 301 Q 309
REMARK 3 ORIGIN FOR THE GROUP (A): 35.486 -203.092 -9.118
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.0635
REMARK 3 T33: 0.1135 T12: 0.0232
REMARK 3 T13: -0.0025 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.0100 L22: 0.0056
REMARK 3 L33: 0.0196 L12: -0.0049
REMARK 3 L13: 0.0076 L23: -0.0091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: -0.0164 S13: -0.0095
REMARK 3 S21: -0.0212 S22: 0.0073 S23: 0.0155
REMARK 3 S31: 0.0193 S32: 0.0041 S33: -0.0334
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 301 R 307
REMARK 3 ORIGIN FOR THE GROUP (A): 64.925 -202.584 3.270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0849 T22: 0.0377
REMARK 3 T33: 0.1135 T12: 0.0361
REMARK 3 T13: 0.0352 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.0156 L22: 0.0198
REMARK 3 L33: 0.0612 L12: -0.0107
REMARK 3 L13: -0.0247 L23: 0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: -0.0104 S13: 0.0116
REMARK 3 S21: -0.0336 S22: -0.0112 S23: -0.0224
REMARK 3 S31: 0.0346 S32: 0.0239 S33: 0.0143
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 3 S 233
REMARK 3 RESIDUE RANGE : S 301 S 306
REMARK 3 ORIGIN FOR THE GROUP (A): 71.858 -203.773 35.228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0691 T22: 0.0661
REMARK 3 T33: 0.1578 T12: 0.0290
REMARK 3 T13: -0.0095 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.0082 L22: 0.0228
REMARK 3 L33: 0.0327 L12: 0.0108
REMARK 3 L13: 0.0137 L23: 0.0263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0038 S13: -0.0009
REMARK 3 S21: 0.0287 S22: 0.0081 S23: -0.0381
REMARK 3 S31: 0.0290 S32: -0.0096 S33: -0.0332
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 2 T 244
REMARK 3 RESIDUE RANGE : T 301 T 313
REMARK 3 ORIGIN FOR THE GROUP (A): 53.948 -207.397 59.474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1235 T22: 0.0438
REMARK 3 T33: 0.1337 T12: 0.0102
REMARK 3 T13: -0.0401 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0162 L22: 0.0065
REMARK 3 L33: 0.0058 L12: 0.0095
REMARK 3 L13: 0.0054 L23: 0.0050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0344 S12: -0.0068 S13: -0.0277
REMARK 3 S21: 0.0183 S22: -0.0147 S23: -0.0206
REMARK 3 S31: 0.0034 S32: -0.0146 S33: -0.0197
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 RESIDUE RANGE : U 301 U 301
REMARK 3 RESIDUE RANGE : U 401 U 408
REMARK 3 ORIGIN FOR THE GROUP (A): 21.627 -209.447 61.118
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.0699
REMARK 3 T33: 0.1332 T12: -0.0080
REMARK 3 T13: -0.0132 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0033 L22: 0.0022
REMARK 3 L33: 0.0013 L12: 0.0015
REMARK 3 L13: -0.0016 L23: -0.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.0136 S13: 0.0103
REMARK 3 S21: 0.0136 S22: 0.0068 S23: 0.0049
REMARK 3 S31: -0.0072 S32: -0.0057 S33: -0.0059
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 226
REMARK 3 RESIDUE RANGE : V 301 V 302
REMARK 3 RESIDUE RANGE : V 401 V 418
REMARK 3 ORIGIN FOR THE GROUP (A): 1.226 -169.666 44.728
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.0842
REMARK 3 T33: 0.1430 T12: -0.0110
REMARK 3 T13: 0.0055 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0086
REMARK 3 L33: 0.0098 L12: 0.0005
REMARK 3 L13: 0.0016 L23: -0.0030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0007 S13: -0.0076
REMARK 3 S21: 0.0086 S22: -0.0094 S23: 0.0203
REMARK 3 S31: 0.0241 S32: 0.0084 S33: -0.0025
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 301 W 311
REMARK 3 ORIGIN FOR THE GROUP (A): 0.046 -167.097 18.196
REMARK 3 T TENSOR
REMARK 3 T11: 0.1113 T22: 0.0775
REMARK 3 T33: 0.1485 T12: -0.0001
REMARK 3 T13: -0.0145 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0335 L22: 0.1162
REMARK 3 L33: 0.0042 L12: 0.0613
REMARK 3 L13: 0.0075 L23: 0.0150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.0045 S13: -0.0027
REMARK 3 S21: -0.0062 S22: 0.0012 S23: 0.0151
REMARK 3 S31: 0.0098 S32: 0.0101 S33: 0.0002
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 195
REMARK 3 RESIDUE RANGE : X 201 X 221
REMARK 3 ORIGIN FOR THE GROUP (A): 23.111 -164.175 -3.698
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.0812
REMARK 3 T33: 0.1353 T12: 0.0056
REMARK 3 T13: -0.0154 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0034 L22: 0.0083
REMARK 3 L33: 0.0006 L12: -0.0033
REMARK 3 L13: 0.0009 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: -0.0068 S13: -0.0156
REMARK 3 S21: -0.0325 S22: -0.0049 S23: 0.0091
REMARK 3 S31: -0.0004 S32: -0.0002 S33: -0.0083
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 301 Y 302
REMARK 3 RESIDUE RANGE : Y 401 Y 415
REMARK 3 ORIGIN FOR THE GROUP (A): 56.981 -160.469 -0.625
REMARK 3 T TENSOR
REMARK 3 T11: 0.1014 T22: 0.0790
REMARK 3 T33: 0.1149 T12: 0.0047
REMARK 3 T13: 0.0290 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0042 L22: 0.0027
REMARK 3 L33: 0.0082 L12: 0.0023
REMARK 3 L13: 0.0058 L23: 0.0038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0052 S13: -0.0087
REMARK 3 S21: 0.0125 S22: 0.0045 S23: -0.0051
REMARK 3 S31: 0.0206 S32: -0.0023 S33: -0.0165
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 RESIDUE RANGE : Z 301 Z 301
REMARK 3 RESIDUE RANGE : Z 401 Z 413
REMARK 3 ORIGIN FOR THE GROUP (A): 72.923 -161.552 25.390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0853 T22: 0.0883
REMARK 3 T33: 0.1450 T12: 0.0102
REMARK 3 T13: 0.0127 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0150 L22: 0.0844
REMARK 3 L33: 0.0227 L12: 0.0329
REMARK 3 L13: -0.0114 L23: -0.0334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0171 S13: -0.0151
REMARK 3 S21: 0.0211 S22: -0.0098 S23: -0.0238
REMARK 3 S31: 0.0142 S32: -0.0014 S33: 0.0021
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 301 a 323
REMARK 3 ORIGIN FOR THE GROUP (A): 61.241 -163.591 57.567
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.0751
REMARK 3 T33: 0.1432 T12: 0.0005
REMARK 3 T13: -0.0110 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.0110 L22: 0.0633
REMARK 3 L33: 0.0113 L12: -0.0131
REMARK 3 L13: -0.0024 L23: 0.0219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.0145 S13: -0.0069
REMARK 3 S21: 0.0214 S22: -0.0071 S23: -0.0068
REMARK 3 S31: 0.0026 S32: -0.0115 S33: 0.0010
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 RESIDUE RANGE : b 201 b 202
REMARK 3 RESIDUE RANGE : b 301 b 310
REMARK 3 ORIGIN FOR THE GROUP (A): 29.472 -169.184 67.753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1349 T22: 0.0859
REMARK 3 T33: 0.1254 T12: -0.0037
REMARK 3 T13: -0.0001 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0542
REMARK 3 L33: 0.0012 L12: 0.0224
REMARK 3 L13: -0.0006 L23: 0.0025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0138 S13: 0.0027
REMARK 3 S21: 0.0289 S22: -0.0026 S23: -0.0123
REMARK 3 S31: 0.0024 S32: -0.0088 S33: -0.0084
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 241198
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 92.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 (%): 66.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR
REMARK 280 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 150.10500
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 300 REMARK: AU CONTAINS ONE BIOLOGICAL ASSEMBLY.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 124890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 212880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -478.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG X 8 OH TYR X 148 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 2 140.27 58.79
REMARK 500 TYR A 97 -65.49 -149.11
REMARK 500 ALA A 249 44.20 -94.96
REMARK 500 ARG B 8 76.21 60.71
REMARK 500 THR B 10 56.16 -114.87
REMARK 500 VAL B 51 90.90 -10.27
REMARK 500 ASN B 220 100.29 -52.73
REMARK 500 ASP B 221 -178.90 72.53
REMARK 500 PRO C 183 105.88 -43.88
REMARK 500 GLN C 202 -98.65 112.43
REMARK 500 ALA C 205 -106.38 -82.54
REMARK 500 ARG D 45 71.59 56.38
REMARK 500 SER E 39 -155.73 -111.28
REMARK 500 ASP E 137 -160.62 -122.83
REMARK 500 ASP E 202 -55.35 67.20
REMARK 500 CYS F 38 -169.17 -110.99
REMARK 500 ASP F 67 -133.61 56.56
REMARK 500 LYS F 100 -54.31 76.89
REMARK 500 ASP F 138 -167.97 -126.61
REMARK 500 SER H 171 -112.67 66.02
REMARK 500 ASN H 194 44.66 -140.85
REMARK 500 GLN I 31 -109.26 57.99
REMARK 500 ASP I 192 33.14 -147.27
REMARK 500 GLN I 203 46.86 -104.05
REMARK 500 ASP J 2 -95.94 -106.70
REMARK 500 VAL J 9 -167.03 -104.89
REMARK 500 SER J 31 32.83 -148.49
REMARK 500 ASP L 32 -115.84 50.52
REMARK 500 LYS L 100 42.71 -108.63
REMARK 500 PHE L 103 68.97 -158.91
REMARK 500 ASN L 165 74.39 51.45
REMARK 500 ASP L 200 -66.01 68.28
REMARK 500 ILE M 5 -77.78 -107.92
REMARK 500 THR M 9 -152.33 -90.66
REMARK 500 ALA M 83 -114.00 -144.99
REMARK 500 LYS N 107 -147.15 63.62
REMARK 500 THR O 2 140.42 58.92
REMARK 500 TYR O 97 -65.85 -149.03
REMARK 500 ALA O 249 44.40 -94.95
REMARK 500 ARG P 8 76.01 60.92
REMARK 500 THR P 10 55.97 -114.68
REMARK 500 VAL P 51 90.88 -10.38
REMARK 500 ASN P 220 100.43 -52.65
REMARK 500 ASP P 221 -178.77 72.50
REMARK 500 PRO Q 183 105.96 -43.93
REMARK 500 GLN Q 202 -98.46 112.59
REMARK 500 ALA Q 205 -106.49 -82.67
REMARK 500 ARG R 45 71.73 56.20
REMARK 500 SER S 39 -155.50 -111.18
REMARK 500 ASP S 137 -160.46 -122.89
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 8 OG1
REMARK 620 2 TYR G 119 O 77.1
REMARK 620 3 ARG G 122 O 77.5 71.3
REMARK 620 4 MET G 125 O 154.6 79.4 85.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA I 174 O
REMARK 620 2 ASP I 177 O 69.2
REMARK 620 3 SER I 180 O 81.1 80.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 106.6
REMARK 620 3 ASP Y 168 O 154.4 92.8
REMARK 620 4 SER Y 171 O 90.5 83.6 74.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 97.2
REMARK 620 3 SER K 171 O 86.8 79.5
REMARK 620 4 ASP W 204 O 103.5 156.4 90.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 97.2
REMARK 620 3 ASP V 166 O 139.3 109.5
REMARK 620 4 SER V 169 O 82.2 86.5 69.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 ASP N 166 O 71.3
REMARK 620 3 SER N 169 O 99.4 68.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 VAL Z 198 O 91.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 b 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL b 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QTR RELATED DB: PDB
REMARK 900 RELATED ID: 4QUX RELATED DB: PDB
REMARK 900 RELATED ID: 4QUY RELATED DB: PDB
REMARK 900 RELATED ID: 4QV0 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV1 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV4 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV5 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV7 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV8 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV9 RELATED DB: PDB
REMARK 900 RELATED ID: 4QVM RELATED DB: PDB
REMARK 900 RELATED ID: 4QVN RELATED DB: PDB
REMARK 900 RELATED ID: 4QVP RELATED DB: PDB
REMARK 900 RELATED ID: 4QVQ RELATED DB: PDB
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 RELATED ID: 4QWR RELATED DB: PDB
REMARK 900 RELATED ID: 4QWS RELATED DB: PDB
REMARK 900 RELATED ID: 4QWU RELATED DB: PDB
REMARK 900 RELATED ID: 4QWX RELATED DB: PDB
DBREF 4QVL A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QVL B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QVL C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QVL D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QVL E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QVL F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QVL G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QVL H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QVL I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QVL J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QVL K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QVL L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QVL M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QVL N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QVL O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QVL P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QVL Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QVL R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QVL S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QVL T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QVL U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QVL V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QVL W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QVL X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QVL Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QVL Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QVL a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QVL b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 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 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 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 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
HET MG G 301 1
HET CL G 302 1
HET BO2 H 301 28
HET MG I 301 1
HET MG J 201 1
HET BO2 K 301 28
HET MG K 302 1
HET BO2 N 201 28
HET MG N 202 1
HET CL N 203 1
HET CL U 301 1
HET BO2 V 301 28
HET MG V 302 1
HET BO2 Y 301 28
HET MG Y 302 1
HET MG Z 301 1
HET BO2 b 201 28
HET CL b 202 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-
HETNAM 2 BO2 YLCARBONYL)-L-PHENYLALANINAMIDE
HETSYN BO2 BORTEZOMIB
FORMUL 29 MG 8(MG 2+)
FORMUL 30 CL 4(CL 1-)
FORMUL 31 BO2 6(C19 H25 B N4 O4)
FORMUL 47 HOH *357(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 ALA A 121 1 16
HELIX 5 5 GLY A 167 TRP A 179 1 13
HELIX 6 6 GLU A 184 VAL A 200 1 17
HELIX 7 7 ASN A 218 LEU A 222 5 5
HELIX 8 8 THR A 239 ALA A 249 1 11
HELIX 9 9 GLY B 1 ASP B 6 5 6
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 GLU C 99 1 24
HELIX 19 19 THR C 103 TYR C 118 1 16
HELIX 20 20 ASN C 165 TYR C 177 1 13
HELIX 21 21 THR C 185 GLU C 199 1 15
HELIX 22 22 SER C 223 GLN C 239 1 17
HELIX 23 23 LEU D 13 LEU D 25 1 13
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 LEU D 113 1 14
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 ALA D 241 1 18
HELIX 30 30 LEU E 18 GLY E 31 1 14
HELIX 31 31 LEU E 76 ASN E 99 1 24
HELIX 32 32 ALA E 103 SER E 121 1 19
HELIX 33 33 ARG E 163 ILE E 179 1 17
HELIX 34 34 ASN E 184 SER E 197 1 14
HELIX 35 35 GLN E 198 LEU E 200 5 3
HELIX 36 36 ASP E 225 ILE E 233 5 9
HELIX 37 37 ASN F 17 GLY F 30 1 14
HELIX 38 38 LEU F 77 LYS F 100 1 24
HELIX 39 39 PRO F 104 HIS F 119 1 16
HELIX 40 40 GLY F 164 HIS F 179 1 16
HELIX 41 41 SER F 184 HIS F 200 1 17
HELIX 42 42 GLU F 201 LYS F 204 5 4
HELIX 43 43 LYS F 228 ASN F 244 1 17
HELIX 44 44 GLY G 2 HIS G 6 5 5
HELIX 45 45 LEU G 16 THR G 26 1 11
HELIX 46 46 ASP G 56 VAL G 60 5 5
HELIX 47 47 PRO G 77 GLY G 100 1 24
HELIX 48 48 PRO G 104 ARG G 122 1 19
HELIX 49 49 LYS G 165 LYS G 181 1 17
HELIX 50 50 SER G 189 GLY G 206 1 18
HELIX 51 51 SER G 228 GLU G 241 1 14
HELIX 52 52 THR H 48 SER H 71 1 24
HELIX 53 53 ARG H 75 TYR H 90 1 16
HELIX 54 54 GLY H 130 TRP H 142 1 13
HELIX 55 55 THR H 147 ASP H 166 1 20
HELIX 56 56 ASP I 2 ILE I 6 5 5
HELIX 57 57 LEU I 55 GLU I 78 1 24
HELIX 58 58 GLU I 82 GLU I 96 1 15
HELIX 59 59 ALA I 141 TYR I 153 1 13
HELIX 60 60 GLU I 158 ASP I 175 1 18
HELIX 61 61 GLY J 51 ASP J 72 1 22
HELIX 62 62 SER J 76 ILE J 92 1 17
HELIX 63 63 TYR J 135 TYR J 148 1 14
HELIX 64 64 THR J 153 MET J 172 1 20
HELIX 65 65 GLY K 48 LYS K 71 1 24
HELIX 66 66 SER K 75 TYR K 90 1 16
HELIX 67 67 GLY K 132 TYR K 144 1 13
HELIX 68 68 SER K 149 ASP K 168 1 20
HELIX 69 69 VAL K 193 GLY K 205 1 13
HELIX 70 70 PHE L 57 HIS L 79 1 23
HELIX 71 71 SER L 85 GLY L 99 1 15
HELIX 72 72 ALA L 142 VAL L 154 1 13
HELIX 73 73 SER L 176 HIS L 195 1 20
HELIX 74 74 ILE M 57 TYR M 76 1 20
HELIX 75 75 GLU M 88 LYS M 106 1 19
HELIX 76 76 GLY M 145 LYS M 157 1 13
HELIX 77 77 ARG M 161 ILE M 165 5 5
HELIX 78 78 THR M 169 ASP M 188 1 20
HELIX 79 79 TRP M 219 ILE M 225 5 7
HELIX 80 80 SER N 48 GLY N 71 1 24
HELIX 81 81 SER N 74 ASN N 89 1 16
HELIX 82 82 GLY N 128 PHE N 133 5 6
HELIX 83 83 ILE N 134 PHE N 142 1 9
HELIX 84 84 SER N 147 ASP N 166 1 20
HELIX 85 85 TYR N 189 GLU N 194 1 6
HELIX 86 86 LEU O 18 GLY O 31 1 14
HELIX 87 87 MET O 78 SER O 96 1 19
HELIX 88 88 TYR O 97 GLY O 102 1 6
HELIX 89 89 PRO O 106 ALA O 121 1 16
HELIX 90 90 GLY O 167 TRP O 179 1 13
HELIX 91 91 GLU O 184 VAL O 200 1 17
HELIX 92 92 ASN O 218 LEU O 222 5 5
HELIX 93 93 THR O 239 ALA O 249 1 11
HELIX 94 94 GLY P 1 ASP P 6 5 6
HELIX 95 95 LEU P 18 SER P 29 1 12
HELIX 96 96 GLU P 57 SER P 61 5 5
HELIX 97 97 LEU P 79 ASN P 102 1 24
HELIX 98 98 PRO P 106 HIS P 124 1 19
HELIX 99 99 ASN P 167 TYR P 179 1 13
HELIX 100 100 LYS P 184 THR P 200 1 17
HELIX 101 101 THR P 206 ASP P 208 5 3
HELIX 102 102 LYS P 230 THR P 241 1 12
HELIX 103 103 ILE Q 15 GLY Q 28 1 14
HELIX 104 104 LEU Q 76 GLU Q 99 1 24
HELIX 105 105 THR Q 103 TYR Q 118 1 16
HELIX 106 106 ASN Q 165 TYR Q 177 1 13
HELIX 107 107 THR Q 185 GLU Q 199 1 15
HELIX 108 108 SER Q 223 GLN Q 239 1 17
HELIX 109 109 LEU R 13 LEU R 25 1 13
HELIX 110 110 GLU R 52 ILE R 56 5 5
HELIX 111 111 ASP R 76 ASP R 96 1 21
HELIX 112 112 ASN R 100 LEU R 113 1 14
HELIX 113 113 GLY R 167 TRP R 179 1 13
HELIX 114 114 THR R 184 MET R 200 1 17
HELIX 115 115 ASP R 224 ALA R 241 1 18
HELIX 116 116 LEU S 18 GLY S 31 1 14
HELIX 117 117 LEU S 76 ASN S 99 1 24
HELIX 118 118 ALA S 103 SER S 121 1 19
HELIX 119 119 ARG S 163 ILE S 179 1 17
HELIX 120 120 ASN S 184 SER S 197 1 14
HELIX 121 121 GLN S 198 LEU S 200 5 3
HELIX 122 122 ASP S 225 ILE S 233 5 9
HELIX 123 123 ASN T 17 GLY T 30 1 14
HELIX 124 124 LEU T 77 LYS T 100 1 24
HELIX 125 125 PRO T 104 HIS T 119 1 16
HELIX 126 126 GLY T 164 HIS T 179 1 16
HELIX 127 127 SER T 184 HIS T 200 1 17
HELIX 128 128 GLU T 201 LYS T 204 5 4
HELIX 129 129 LYS T 228 ASN T 244 1 17
HELIX 130 130 GLY U 2 HIS U 6 5 5
HELIX 131 131 LEU U 16 THR U 26 1 11
HELIX 132 132 ASP U 56 VAL U 60 5 5
HELIX 133 133 PRO U 77 GLY U 100 1 24
HELIX 134 134 PRO U 104 ARG U 122 1 19
HELIX 135 135 LYS U 165 LYS U 181 1 17
HELIX 136 136 SER U 189 GLY U 206 1 18
HELIX 137 137 SER U 228 GLU U 241 1 14
HELIX 138 138 THR V 48 SER V 71 1 24
HELIX 139 139 ARG V 75 TYR V 90 1 16
HELIX 140 140 GLY V 130 TRP V 142 1 13
HELIX 141 141 THR V 147 ASP V 166 1 20
HELIX 142 142 ASP W 2 ILE W 6 5 5
HELIX 143 143 LEU W 55 GLU W 78 1 24
HELIX 144 144 GLU W 82 GLU W 96 1 15
HELIX 145 145 ALA W 141 TYR W 153 1 13
HELIX 146 146 GLU W 158 ASP W 175 1 18
HELIX 147 147 GLY X 51 ASP X 72 1 22
HELIX 148 148 SER X 76 ILE X 92 1 17
HELIX 149 149 TYR X 135 TYR X 148 1 14
HELIX 150 150 THR X 153 MET X 172 1 20
HELIX 151 151 GLY Y 48 LYS Y 71 1 24
HELIX 152 152 SER Y 75 TYR Y 90 1 16
HELIX 153 153 GLY Y 132 TYR Y 144 1 13
HELIX 154 154 SER Y 149 ASP Y 168 1 20
HELIX 155 155 VAL Y 193 GLY Y 205 1 13
HELIX 156 156 PHE Z 57 HIS Z 79 1 23
HELIX 157 157 SER Z 85 GLY Z 99 1 15
HELIX 158 158 ALA Z 142 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 LYS a 157 1 13
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 ILE a 225 5 7
HELIX 166 166 SER b 48 GLY b 71 1 24
HELIX 167 167 SER b 74 ASN b 89 1 16
HELIX 168 168 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 5 SER A 65 THR A 68 0
SHEET 2 B 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 B 5 VAL A 132 ASP A 140 -1 O ALA A 137 N GLY A 72
SHEET 4 B 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 B 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 C 6 TYR A 224 THR A 225 0
SHEET 2 C 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 C 6 VAL H 173 GLU H 179 -1 N VAL H 177 O GLU H 185
SHEET 4 C 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 C 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 C 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 D 5 ALA B 161 VAL B 164 0
SHEET 2 D 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 D 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 D 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 D 5 TYR B 225 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 E 5 LEU B 65 LYS B 67 0
SHEET 2 E 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 E 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 E 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 E 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 F 5 ALA C 159 ILE C 162 0
SHEET 2 F 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 F 5 VAL C 40 GLU C 45 -1 O VAL C 41 N VAL C 34
SHEET 4 F 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 F 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 G 5 SER C 63 LYS C 64 0
SHEET 2 G 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 G 5 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 G 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 G 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 H 5 ALA D 161 ILE D 164 0
SHEET 2 H 5 ALA D 29 ALA D 33 -1 N GLY D 31 O LYS D 162
SHEET 3 H 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 H 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 H 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 I 5 ILE D 59 ASP D 63 0
SHEET 2 I 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 I 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 I 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 I 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 J 5 GLY E 157 ILE E 160 0
SHEET 2 J 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 J 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 J 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 J 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 K 5 ILE E 62 ASP E 66 0
SHEET 2 K 5 MET E 69 GLY E 75 -1 O MET E 69 N ASP E 66
SHEET 3 K 5 VAL E 129 ASP E 137 -1 O GLY E 130 N ALA E 74
SHEET 4 K 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 K 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 L 5 GLY F 158 THR F 161 0
SHEET 2 L 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 L 5 GLY F 41 LEU F 49 -1 O ALA F 45 N ILE F 34
SHEET 4 L 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 L 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 M 5 GLN F 64 VAL F 66 0
SHEET 2 M 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 M 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 M 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 M 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 N 5 ALA G 159 THR G 162 0
SHEET 2 N 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 N 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 N 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 N 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
SHEET 1 O 5 ILE G 63 CYS G 65 0
SHEET 2 O 5 GLY G 71 ASN G 75 -1 O MET G 72 N PHE G 64
SHEET 3 O 5 ILE G 131 ASP G 138 -1 O VAL G 135 N GLY G 71
SHEET 4 O 5 GLY G 142 THR G 148 -1 O TYR G 146 N PHE G 134
SHEET 5 O 5 TYR G 154 TYR G 157 -1 O TYR G 157 N ILE G 145
SHEET 1 P 2 SER H 20 GLN H 22 0
SHEET 2 P 2 ILE H 25 ASP H 28 -1 O ASP H 28 N SER H 20
SHEET 1 Q 5 LEU H 34 SER H 38 0
SHEET 2 Q 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 Q 5 ALA H 96 ASP H 104 -1 O TYR H 97 N ALA H 46
SHEET 4 Q 5 GLY H 107 ILE H 113 -1 O ILE H 113 N LEU H 98
SHEET 5 Q 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 R 6 VAL H 212 ILE H 217 0
SHEET 2 R 6 GLU I 193 LEU I 199 -1 O TYR I 198 N LEU H 213
SHEET 3 R 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 R 6 CYS I 19 ASP I 25 -1 N VAL I 20 O ILE I 189
SHEET 5 R 6 ILE I 10 GLY I 16 -1 N VAL I 12 O ALA I 23
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 5 ILE I 42 TYR I 45 0
SHEET 2 T 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 T 5 VAL I 104 ILE I 111 -1 O VAL I 107 N GLY I 51
SHEET 4 T 5 PRO I 118 PHE I 123 -1 O ALA I 121 N VAL I 108
SHEET 5 T 5 ILE I 129 ASP I 130 -1 O ASP I 130 N GLY I 122
SHEET 1 U 5 TYR J 130 HIS J 133 0
SHEET 2 U 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 U 5 SER J 12 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 U 5 VAL J 179 ASP J 185 -1 O ILE J 180 N SER J 17
SHEET 5 U 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 V 2 VAL J 21 ARG J 23 0
SHEET 2 V 2 SER J 26 LYS J 29 -1 O SER J 26 N ARG J 23
SHEET 1 W 5 THR J 35 SER J 39 0
SHEET 2 W 5 THR J 42 GLY J 48 -1 O THR J 42 N SER J 39
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 ILE J 119 N VAL J 102
SHEET 5 W 5 LYS J 125 LEU J 128 -1 O VAL J 126 N GLN J 118
SHEET 1 X 5 ILE K 126 VAL K 129 0
SHEET 2 X 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 129
SHEET 3 X 5 GLY K 11 VAL K 16 -1 O ALA K 15 N LEU K 4
SHEET 4 X 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 X 5 GLY K 184 ASP K 192 -1 O HIS K 188 N LEU K 177
SHEET 1 Y 2 ALA K 20 ALA K 22 0
SHEET 2 Y 2 TRP K 25 SER K 28 -1 O TRP K 25 N ALA K 22
SHEET 1 Z 5 VAL K 34 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 LYS K 123 -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 GLY L 14 O ARG L 137
SHEET 3 AA 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AA 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AA 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AB 2 ASN L 29 THR L 31 0
SHEET 2 AB 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AC 5 VAL L 43 ASP L 45 0
SHEET 2 AC 5 VAL L 51 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 TYR M 16 -1 N SER M 13 O LEU M 142
SHEET 3 AF 5 GLY M 19 ASP M 25 -1 O GLY M 19 N TYR M 16
SHEET 4 AF 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AF 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 PHE N 8 -1 N ALA N 5 O ALA N 125
SHEET 3 AG 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AG 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AG 5 GLY N 182 PHE N 188 -1 O GLU N 184 N VAL N 177
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 CYS N 43 N THR N 35
SHEET 3 AI 5 ALA N 95 TYR N 102 -1 O GLY N 96 N SER N 46
SHEET 4 AI 5 GLY N 108 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 ALA O 73 N SER O 65
SHEET 3 AL 5 VAL O 132 ASP O 140 -1 O ALA O 137 N GLY O 72
SHEET 4 AL 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
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 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AM 6 TYR V 124 LEU V 127 -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 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AN 5 TYR P 225 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 ILE P 72 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 TYR P 148 N TYR P 136
SHEET 5 AO 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AP 5 ALA Q 159 ILE Q 162 0
SHEET 2 AP 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
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 VAL Q 213 N VAL Q 40
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 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AQ 5 LYS Q 144 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 GLY R 31 O LYS R 162
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 CYS R 68 N VAL R 60
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 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AU 5 ILE S 62 ASP S 66 0
SHEET 2 AU 5 MET S 69 GLY S 75 -1 O MET S 69 N ASP S 66
SHEET 3 AU 5 VAL S 129 ASP S 137 -1 O GLY S 130 N ALA S 74
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 GLY T 35 O ALA T 159
SHEET 3 AV 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AV 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AV 5 HIS T 224 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 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AW 5 GLY T 141 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 GLY U 217 N VAL U 44
SHEET 5 AX 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AY 2 SER V 20 GLN V 22 0
SHEET 2 AY 2 ILE V 25 ASP V 28 -1 O ASP V 28 N SER V 20
SHEET 1 AZ 5 LEU V 34 SER V 38 0
SHEET 2 AZ 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AZ 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AZ 5 GLY V 107 ILE V 113 -1 O ILE V 113 N LEU V 98
SHEET 5 AZ 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 BA 6 VAL V 212 ILE V 217 0
SHEET 2 BA 6 GLU W 193 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 BA 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 BA 6 CYS W 19 ASP W 25 -1 N VAL W 20 O ILE W 189
SHEET 5 BA 6 ILE W 10 GLY W 16 -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 5 ILE W 42 TYR W 45 0
SHEET 2 BC 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 BC 5 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 BC 5 PRO W 118 PHE W 123 -1 O ALA W 121 N VAL W 108
SHEET 5 BC 5 ILE W 129 ASP W 130 -1 O ASP W 130 N GLY W 122
SHEET 1 BD 5 TYR X 130 HIS X 133 0
SHEET 2 BD 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 BD 5 SER X 12 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O ILE X 180 N SER X 17
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 BE 2 VAL X 21 ARG X 23 0
SHEET 2 BE 2 SER X 26 LYS X 29 -1 O LYS X 29 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 THR X 42 N SER X 39
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 LEU X 128 -1 O VAL X 126 N GLN X 118
SHEET 1 BG 5 ILE Y 126 VAL Y 129 0
SHEET 2 BG 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O 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 188 N LEU Y 177
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 BI 5 VAL Y 34 GLU Y 36 0
SHEET 2 BI 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BI 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BI 5 GLY Y 109 ASP Y 116 -1 O VAL Y 115 N THR Y 99
SHEET 5 BI 5 ARG Y 121 LYS Y 123 -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 GLY Z 14 O ARG Z 137
SHEET 3 BJ 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 BJ 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 BJ 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 BK 2 ASN Z 29 THR Z 31 0
SHEET 2 BK 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 BL 5 VAL Z 43 ASP Z 45 0
SHEET 2 BL 5 VAL Z 51 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 PRO a 44 -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 TYR a 16 -1 N SER a 13 O LEU a 142
SHEET 3 BO 5 GLY a 19 ASP a 25 -1 O GLY a 19 N TYR a 16
SHEET 4 BO 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 BO 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 BP 5 TYR b 124 ALA b 127 0
SHEET 2 BP 5 ILE b 3 PHE b 8 -1 N ALA b 5 O ALA b 125
SHEET 3 BP 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 BP 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 BP 5 GLY b 182 PHE b 188 -1 O GLU b 184 N VAL b 177
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 CYS b 43 N THR b 35
SHEET 3 BR 5 ALA b 95 TYR b 102 -1 O GLY b 96 N SER b 46
SHEET 4 BR 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 BR 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR H 1 B26 BO2 H 301 1555 1555 1.44
LINK OG1 THR K 1 B26 BO2 K 301 1555 1555 1.44
LINK OG1 THR N 1 B26 BO2 N 201 1555 1555 1.44
LINK OG1 THR V 1 B26 BO2 V 301 1555 1555 1.43
LINK OG1 THR Y 1 B26 BO2 Y 301 1555 1555 1.44
LINK OG1 THR b 1 B26 BO2 b 201 1555 1555 1.43
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.58
LINK O TYR G 119 MG MG G 301 1555 1555 2.80
LINK O ARG G 122 MG MG G 301 1555 1555 2.57
LINK O MET G 125 MG MG G 301 1555 1555 2.19
LINK O ALA I 174 MG MG I 301 1555 1555 2.75
LINK O ASP I 177 MG MG I 301 1555 1555 2.34
LINK O SER I 180 MG MG I 301 1555 1555 2.76
LINK O ASP I 204 MG MG Y 302 1555 1555 2.27
LINK O ALA K 165 MG MG K 302 1555 1555 2.37
LINK O ASP K 168 MG MG K 302 1555 1555 2.17
LINK O SER K 171 MG MG K 302 1555 1555 2.75
LINK MG MG K 302 O ASP W 204 1555 1555 2.36
LINK OXT ASP L 222 MG MG V 302 1555 1555 2.16
LINK O ILE N 163 MG MG N 202 1555 1555 2.62
LINK O ASP N 166 MG MG N 202 1555 1555 2.85
LINK O SER N 169 MG MG N 202 1555 1555 2.50
LINK O ILE V 163 MG MG V 302 1555 1555 2.15
LINK O ASP V 166 MG MG V 302 1555 1555 2.27
LINK O SER V 169 MG MG V 302 1555 1555 2.77
LINK O ALA Y 165 MG MG Y 302 1555 1555 2.43
LINK O ASP Y 168 MG MG Y 302 1555 1555 2.30
LINK O SER Y 171 MG MG Y 302 1555 1555 2.86
LINK O THR Z 192 MG MG Z 301 1555 1555 2.98
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.45
SITE 1 AC1 5 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 5 MET G 125
SITE 1 AC2 3 ARG G 111 ASN G 114 TYR H 69
SITE 1 AC3 9 THR H 1 SER H 20 THR H 21 GLN H 22
SITE 2 AC3 9 GLY H 45 GLY H 47 ALA H 49 THR H 52
SITE 3 AC3 9 ASP I 124
SITE 1 AC4 3 ALA I 174 ASP I 177 SER I 180
SITE 1 AC5 1 GLN J 118
SITE 1 AC6 7 THR K 1 ALA K 20 THR K 21 MET K 45
SITE 2 AC6 7 GLY K 47 ALA K 49 ASP L 126
SITE 1 AC7 5 ALA K 165 ASP K 168 ALA K 169 SER K 171
SITE 2 AC7 5 ASP W 204
SITE 1 AC8 9 HIS H 114 SER H 118 THR N 1 THR N 20
SITE 2 AC8 9 THR N 21 THR N 22 ARG N 45 GLY N 47
SITE 3 AC8 9 ALA N 49
SITE 1 AC9 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC9 5 LEU a 34
SITE 1 BC1 3 THR N 31 ARG N 45 GLN N 53
SITE 1 BC2 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 BC3 9 THR V 1 SER V 20 THR V 21 GLN V 22
SITE 2 BC3 9 GLY V 45 GLY V 47 ALA V 49 THR V 52
SITE 3 BC3 9 ASP W 124
SITE 1 BC4 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 BC5 7 THR Y 1 ALA Y 20 THR Y 21 MET Y 45
SITE 2 BC5 7 GLY Y 47 ALA Y 49 ASP Z 126
SITE 1 BC6 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 BC6 5 SER Y 171
SITE 1 BC7 5 ARG Z 28 THR Z 192 HIS Z 195 VAL Z 198
SITE 2 BC7 5 ASP Z 222
SITE 1 BC8 9 HIS V 114 SER V 118 THR b 1 THR b 20
SITE 2 BC8 9 THR b 21 THR b 22 ARG b 45 GLY b 47
SITE 3 BC8 9 ALA b 49
SITE 1 BC9 2 ARG b 45 GLN b 53
CRYST1 134.910 300.210 144.760 90.00 112.85 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 0.007412 0.000000 0.003123 0.00000
SCALE2 0.000000 0.003331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007496 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 -0.999581 -0.002243 0.028872 67.17099 1
MTRIX2 2 -0.002809 -0.984788 -0.173738 -288.64862 1
MTRIX3 2 0.028822 -0.173746 0.984369 -25.97725 1
(ATOM LINES ARE NOT SHOWN.)
END