HEADER HYDROLASE/HYDROLASE INHIBITOR 16-JUL-14 4QW3
TITLE YCP BETA5-C63F MUTANT IN COMPLEX WITH BORTEZOMIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 EC: 3.4.25.1;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 8 CHAIN: B, P;
COMPND 9 EC: 3.4.25.1;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 12 CHAIN: C, Q;
COMPND 13 EC: 3.4.25.1;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 16 CHAIN: D, R;
COMPND 17 EC: 3.4.25.1;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 20 CHAIN: E, S;
COMPND 21 EC: 3.4.25.1;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 24 CHAIN: F, T;
COMPND 25 EC: 3.4.25.1;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 28 CHAIN: G, U;
COMPND 29 EC: 3.4.25.1;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 32 CHAIN: H, V;
COMPND 33 EC: 3.4.25.1;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 36 CHAIN: I, W;
COMPND 37 EC: 3.4.25.1;
COMPND 38 MOL_ID: 10;
COMPND 39 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 40 CHAIN: J, X;
COMPND 41 EC: 3.4.25.1;
COMPND 42 MOL_ID: 11;
COMPND 43 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 44 CHAIN: K, Y;
COMPND 45 EC: 3.4.25.1;
COMPND 46 ENGINEERED: YES;
COMPND 47 MOL_ID: 12;
COMPND 48 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 49 CHAIN: L, Z;
COMPND 50 EC: 3.4.25.1;
COMPND 51 MOL_ID: 13;
COMPND 52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 53 CHAIN: M, a;
COMPND 54 EC: 3.4.25.1;
COMPND 55 MOL_ID: 14;
COMPND 56 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 57 CHAIN: N, b;
COMPND 58 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 4QW3 1 REMARK SEQADV LINK
REVDAT 2 18-FEB-15 4QW3 1 JRNL
REVDAT 1 04-FEB-15 4QW3 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. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 226393
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11916
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16233
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE SET COUNT : 854
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49376
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 177
REMARK 3 SOLVENT ATOMS : 253
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.26000
REMARK 3 B22 (A**2) : -8.34000
REMARK 3 B33 (A**2) : 2.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.73000
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): 0.302
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.254
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50466 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48206 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68278 ; 0.848 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES):110986 ; 0.693 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6314 ; 4.977 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2254 ;33.961 ;24.419
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8752 ;13.948 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;13.238 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7686 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57266 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11332 ; 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 ; 3.198 ; 6.268
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25345 ; 3.197 ; 6.268
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31630 ; 4.284 ; 9.385
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31631 ; 4.284 ; 9.385
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25120 ; 3.050 ; 6.661
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25120 ; 3.050 ; 6.661
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36648 ; 3.862 ; 9.836
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 53617 ; 4.902 ;48.702
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 53598 ; 4.899 ;48.707
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98672 ; 1.656 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 198 ;29.821 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97824 ;20.151 ; 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 307
REMARK 3 ORIGIN FOR THE GROUP (A): 67.9414 -91.7879 46.5041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1160 T22: 0.0954
REMARK 3 T33: 0.1205 T12: -0.0058
REMARK 3 T13: -0.0086 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0101 L22: 0.0492
REMARK 3 L33: 0.0137 L12: -0.0104
REMARK 3 L13: 0.0071 L23: -0.0250
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: 0.0064 S13: -0.0225
REMARK 3 S21: -0.0105 S22: 0.0036 S23: -0.0212
REMARK 3 S31: -0.0016 S32: -0.0062 S33: 0.0032
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7440 -87.6115 16.8765
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.0990
REMARK 3 T33: 0.1205 T12: -0.0097
REMARK 3 T13: 0.0280 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0074
REMARK 3 L33: 0.0013 L12: -0.0001
REMARK 3 L13: -0.0005 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: 0.0017 S13: -0.0039
REMARK 3 S21: -0.0192 S22: -0.0036 S23: 0.0129
REMARK 3 S31: 0.0098 S32: -0.0031 S33: 0.0069
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 305
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4072 -86.8879 1.5248
REMARK 3 T TENSOR
REMARK 3 T11: 0.1479 T22: 0.0920
REMARK 3 T33: 0.1223 T12: 0.0031
REMARK 3 T13: -0.0044 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.0048 L22: 0.0051
REMARK 3 L33: 0.0051 L12: 0.0032
REMARK 3 L13: -0.0015 L23: -0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0086 S12: 0.0026 S13: 0.0135
REMARK 3 S21: -0.0075 S22: 0.0053 S23: 0.0233
REMARK 3 S31: 0.0194 S32: 0.0055 S33: -0.0139
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 305
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0552 -89.4989 14.1252
REMARK 3 T TENSOR
REMARK 3 T11: 0.1047 T22: 0.0642
REMARK 3 T33: 0.1322 T12: 0.0135
REMARK 3 T13: -0.0145 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0023 L22: 0.0046
REMARK 3 L33: 0.0045 L12: -0.0013
REMARK 3 L13: -0.0029 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0077 S13: -0.0047
REMARK 3 S21: -0.0122 S22: -0.0052 S23: 0.0216
REMARK 3 S31: -0.0071 S32: 0.0149 S33: -0.0026
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 302
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2256 -94.0224 46.0469
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.0963
REMARK 3 T33: 0.1465 T12: 0.0032
REMARK 3 T13: 0.0283 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.0027 L22: 0.0081
REMARK 3 L33: 0.0032 L12: 0.0027
REMARK 3 L13: 0.0022 L23: 0.0033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: -0.0035 S13: 0.0013
REMARK 3 S21: -0.0055 S22: -0.0003 S23: 0.0293
REMARK 3 S31: -0.0098 S32: 0.0080 S33: 0.0096
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 311
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1349 -94.7040 70.3004
REMARK 3 T TENSOR
REMARK 3 T11: 0.1264 T22: 0.0867
REMARK 3 T33: 0.1113 T12: 0.0033
REMARK 3 T13: 0.0339 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 0.0009
REMARK 3 L33: 0.0015 L12: -0.0006
REMARK 3 L13: -0.0003 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.0069 S13: -0.0074
REMARK 3 S21: 0.0076 S22: -0.0041 S23: 0.0085
REMARK 3 S31: 0.0083 S32: 0.0046 S33: 0.0080
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): 48.6339 -93.1191 71.6573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.0714
REMARK 3 T33: 0.0987 T12: -0.0003
REMARK 3 T13: 0.0086 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.0244 L22: 0.0173
REMARK 3 L33: 0.0573 L12: 0.0011
REMARK 3 L13: -0.0253 L23: -0.0044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: 0.0175 S13: 0.0072
REMARK 3 S21: 0.0372 S22: -0.0165 S23: -0.0135
REMARK 3 S31: 0.0142 S32: 0.0113 S33: 0.0058
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 414
REMARK 3 ORIGIN FOR THE GROUP (A): 68.3903-129.3379 47.8283
REMARK 3 T TENSOR
REMARK 3 T11: 0.1022 T22: 0.0884
REMARK 3 T33: 0.1208 T12: -0.0034
REMARK 3 T13: -0.0159 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.0084 L22: 0.0650
REMARK 3 L33: 0.0030 L12: 0.0180
REMARK 3 L13: -0.0020 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: 0.0043 S13: 0.0057
REMARK 3 S21: 0.0495 S22: -0.0091 S23: -0.0385
REMARK 3 S31: -0.0073 S32: -0.0141 S33: -0.0041
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 RESIDUE RANGE : I 301 I 309
REMARK 3 ORIGIN FOR THE GROUP (A): 69.1344-127.2506 21.4116
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.0958
REMARK 3 T33: 0.1236 T12: -0.0055
REMARK 3 T13: 0.0196 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: 0.1058
REMARK 3 L33: 0.0107 L12: -0.0122
REMARK 3 L13: 0.0011 L23: -0.0174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: 0.0013 S13: 0.0013
REMARK 3 S21: -0.0237 S22: -0.0062 S23: -0.0291
REMARK 3 S31: -0.0223 S32: -0.0079 S33: 0.0018
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 309
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6572-126.2204 -0.0779
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.0817
REMARK 3 T33: 0.0922 T12: -0.0011
REMARK 3 T13: -0.0047 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.0983 L22: 0.5134
REMARK 3 L33: 0.5670 L12: -0.1929
REMARK 3 L13: -0.1564 L23: 0.5087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0666 S12: -0.0044 S13: 0.0125
REMARK 3 S21: -0.0422 S22: -0.0340 S23: -0.0147
REMARK 3 S31: 0.0489 S32: -0.0298 S33: -0.0325
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 301
REMARK 3 RESIDUE RANGE : K 401 K 412
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9356-130.3573 2.9478
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.0826
REMARK 3 T33: 0.1199 T12: -0.0067
REMARK 3 T13: -0.0242 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.0082 L22: 0.0494
REMARK 3 L33: 0.0071 L12: -0.0177
REMARK 3 L13: -0.0019 L23: 0.0115
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: 0.0001 S13: -0.0178
REMARK 3 S21: -0.0079 S22: 0.0136 S23: 0.0221
REMARK 3 S31: -0.0081 S32: 0.0198 S33: -0.0139
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 310
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4996-133.8340 28.9376
REMARK 3 T TENSOR
REMARK 3 T11: 0.0804 T22: 0.0932
REMARK 3 T33: 0.1459 T12: 0.0047
REMARK 3 T13: 0.0055 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.0053 L22: 0.0022
REMARK 3 L33: 0.0054 L12: 0.0005
REMARK 3 L13: -0.0010 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: -0.0169 S13: 0.0169
REMARK 3 S21: 0.0025 S22: 0.0042 S23: 0.0155
REMARK 3 S31: -0.0173 S32: 0.0110 S33: 0.0013
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 318
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8155-137.4677 60.6875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1086 T22: 0.0952
REMARK 3 T33: 0.1165 T12: -0.0019
REMARK 3 T13: 0.0257 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.0088 L22: 0.1505
REMARK 3 L33: 0.0024 L12: -0.0239
REMARK 3 L13: 0.0007 L23: 0.0067
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: 0.0053 S13: 0.0198
REMARK 3 S21: 0.0299 S22: -0.0185 S23: 0.0006
REMARK 3 S31: 0.0051 S32: 0.0114 S33: 0.0068
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 305
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6772-133.8057 71.0555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1638 T22: 0.0945
REMARK 3 T33: 0.1125 T12: -0.0059
REMARK 3 T13: -0.0020 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0306 L22: 0.0691
REMARK 3 L33: 0.0045 L12: -0.0417
REMARK 3 L13: -0.0112 L23: 0.0174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: 0.0106 S13: -0.0015
REMARK 3 S21: 0.0286 S22: -0.0129 S23: 0.0070
REMARK 3 S31: 0.0036 S32: -0.0015 S33: 0.0010
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3951-206.1942 37.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0856 T22: 0.0881
REMARK 3 T33: 0.1317 T12: -0.0124
REMARK 3 T13: -0.0178 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.0522 L22: 0.0372
REMARK 3 L33: 0.0056 L12: 0.0419
REMARK 3 L13: -0.0110 L23: -0.0083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: 0.0186 S13: 0.0000
REMARK 3 S21: -0.0154 S22: 0.0003 S23: 0.0085
REMARK 3 S31: 0.0121 S32: -0.0022 S33: 0.0151
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8640-205.0756 7.1161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.0836
REMARK 3 T33: 0.1196 T12: -0.0040
REMARK 3 T13: -0.0340 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.0231 L22: 0.0060
REMARK 3 L33: 0.0495 L12: -0.0021
REMARK 3 L13: 0.0333 L23: -0.0057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.0023 S13: 0.0075
REMARK 3 S21: -0.0164 S22: -0.0022 S23: -0.0133
REMARK 3 S31: -0.0001 S32: 0.0068 S33: 0.0110
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2425-203.2921 -8.7731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.0643
REMARK 3 T33: 0.0810 T12: 0.0076
REMARK 3 T13: -0.0073 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.0037 L22: 0.0045
REMARK 3 L33: 0.0044 L12: -0.0036
REMARK 3 L13: -0.0022 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.0013 S13: -0.0016
REMARK 3 S21: -0.0212 S22: -0.0090 S23: 0.0106
REMARK 3 S31: -0.0128 S32: 0.0134 S33: -0.0081
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 305
REMARK 3 ORIGIN FOR THE GROUP (A): 65.7300-202.8777 3.7512
REMARK 3 T TENSOR
REMARK 3 T11: 0.0454 T22: 0.0436
REMARK 3 T33: 0.0904 T12: 0.0309
REMARK 3 T13: 0.0152 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 0.0084 L22: 0.0987
REMARK 3 L33: 0.0323 L12: -0.0261
REMARK 3 L13: 0.0136 L23: -0.0556
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.0010 S13: 0.0246
REMARK 3 S21: -0.0594 S22: -0.0294 S23: -0.0596
REMARK 3 S31: 0.0353 S32: 0.0192 S33: 0.0220
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 303
REMARK 3 ORIGIN FOR THE GROUP (A): 72.5817-203.9468 35.6662
REMARK 3 T TENSOR
REMARK 3 T11: 0.0633 T22: 0.0654
REMARK 3 T33: 0.1158 T12: 0.0219
REMARK 3 T13: -0.0086 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.0037 L22: 0.0113
REMARK 3 L33: 0.0073 L12: 0.0010
REMARK 3 L13: 0.0008 L23: -0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: 0.0033 S13: 0.0044
REMARK 3 S21: 0.0067 S22: -0.0051 S23: -0.0258
REMARK 3 S31: 0.0080 S32: -0.0041 S33: -0.0075
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 304
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6359-207.4682 59.9907
REMARK 3 T TENSOR
REMARK 3 T11: 0.1246 T22: 0.0663
REMARK 3 T33: 0.1152 T12: 0.0023
REMARK 3 T13: -0.0422 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.0106 L22: 0.0045
REMARK 3 L33: 0.0075 L12: 0.0051
REMARK 3 L13: -0.0085 L23: -0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: 0.0055 S13: -0.0075
REMARK 3 S21: 0.0176 S22: -0.0176 S23: -0.0152
REMARK 3 S31: -0.0234 S32: -0.0095 S33: -0.0026
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): 22.2392-209.4453 61.6217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1479 T22: 0.0762
REMARK 3 T33: 0.1179 T12: -0.0083
REMARK 3 T13: -0.0176 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.0013 L22: 0.0026
REMARK 3 L33: 0.0033 L12: 0.0008
REMARK 3 L13: -0.0002 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.0087 S13: 0.0068
REMARK 3 S21: 0.0047 S22: 0.0053 S23: 0.0162
REMARK 3 S31: 0.0082 S32: 0.0044 S33: -0.0117
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 301
REMARK 3 RESIDUE RANGE : V 401 V 411
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1067-169.5073 44.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: 0.0863
REMARK 3 T33: 0.1319 T12: -0.0020
REMARK 3 T13: 0.0054 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.0086 L22: 0.0625
REMARK 3 L33: 0.0175 L12: 0.0189
REMARK 3 L13: 0.0111 L23: 0.0228
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: -0.0029 S13: -0.0037
REMARK 3 S21: 0.0326 S22: -0.0081 S23: 0.0294
REMARK 3 S31: 0.0300 S32: 0.0122 S33: -0.0115
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 304
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8754-166.9368 18.5851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1140 T22: 0.0792
REMARK 3 T33: 0.1338 T12: -0.0058
REMARK 3 T13: -0.0193 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0047 L22: 0.1203
REMARK 3 L33: 0.0115 L12: 0.0217
REMARK 3 L13: -0.0011 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0000 S12: -0.0050 S13: 0.0089
REMARK 3 S21: -0.0420 S22: -0.0006 S23: 0.0423
REMARK 3 S31: 0.0271 S32: 0.0183 S33: 0.0006
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 211
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0066-164.1831 -3.2404
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.0872
REMARK 3 T33: 0.1105 T12: 0.0111
REMARK 3 T13: -0.0229 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.0065 L22: 0.0033
REMARK 3 L33: 0.0014 L12: -0.0012
REMARK 3 L13: -0.0007 L23: -0.0013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0121 S13: -0.0206
REMARK 3 S21: -0.0123 S22: -0.0090 S23: 0.0132
REMARK 3 S31: -0.0043 S32: 0.0092 S33: -0.0028
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 408
REMARK 3 ORIGIN FOR THE GROUP (A): 57.7761-160.6221 -0.1431
REMARK 3 T TENSOR
REMARK 3 T11: 0.1056 T22: 0.0847
REMARK 3 T33: 0.0952 T12: 0.0079
REMARK 3 T13: 0.0301 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.0311 L22: 0.0887
REMARK 3 L33: 0.0155 L12: 0.0409
REMARK 3 L13: 0.0003 L23: -0.0185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.0013 S13: -0.0105
REMARK 3 S21: -0.0425 S22: 0.0143 S23: -0.0164
REMARK 3 S31: 0.0197 S32: -0.0138 S33: -0.0207
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 414
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6258-161.7054 25.7479
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.0869
REMARK 3 T33: 0.1327 T12: 0.0112
REMARK 3 T13: 0.0039 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0055 L22: 0.1141
REMARK 3 L33: 0.0137 L12: 0.0218
REMARK 3 L13: -0.0031 L23: -0.0258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.0090 S13: -0.0074
REMARK 3 S21: 0.0069 S22: 0.0017 S23: -0.0075
REMARK 3 S31: 0.0203 S32: -0.0123 S33: -0.0028
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 325
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9133-163.6610 57.8577
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.0851
REMARK 3 T33: 0.1206 T12: 0.0038
REMARK 3 T13: -0.0244 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0060 L22: 0.1821
REMARK 3 L33: 0.0037 L12: -0.0064
REMARK 3 L13: -0.0033 L23: 0.0078
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: 0.0119 S13: -0.0206
REMARK 3 S21: 0.0222 S22: -0.0018 S23: -0.0167
REMARK 3 S31: 0.0023 S32: -0.0167 S33: 0.0011
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2399-169.1267 68.0745
REMARK 3 T TENSOR
REMARK 3 T11: 0.1561 T22: 0.0958
REMARK 3 T33: 0.1135 T12: -0.0026
REMARK 3 T13: -0.0034 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0087 L22: 0.0033
REMARK 3 L33: 0.0052 L12: 0.0040
REMARK 3 L13: 0.0052 L23: 0.0028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: 0.0033 S13: -0.0044
REMARK 3 S21: 0.0192 S22: -0.0103 S23: -0.0029
REMARK 3 S31: 0.0077 S32: -0.0082 S33: -0.0122
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 4QW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-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 : 238309
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
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 : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 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 149.98000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 127090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 215250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -471.0 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 ILE J 25 OH TYR X 139 2.11
REMARK 500 O ARG X 8 OH TYR X 148 2.12
REMARK 500 OH TYR J 139 O ILE X 25 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 2 139.96 61.69
REMARK 500 TYR A 97 -65.86 -146.47
REMARK 500 ALA A 249 48.27 -96.33
REMARK 500 ARG B 8 75.13 55.92
REMARK 500 THR B 10 51.36 -117.63
REMARK 500 VAL B 51 91.41 -4.95
REMARK 500 ASN B 220 100.30 -53.82
REMARK 500 ASP B 221 -178.31 71.16
REMARK 500 PRO C 183 108.57 -48.48
REMARK 500 GLN C 202 -97.03 114.50
REMARK 500 ALA C 205 -105.24 -81.96
REMARK 500 ARG D 45 75.13 58.13
REMARK 500 SER E 39 -154.43 -108.64
REMARK 500 ASP E 137 -159.13 -124.73
REMARK 500 ASP E 202 -60.98 67.45
REMARK 500 ASP F 67 -128.52 57.29
REMARK 500 LYS F 100 -58.00 73.28
REMARK 500 LYS G 165 45.26 -106.00
REMARK 500 SER H 171 -115.39 64.47
REMARK 500 ASN H 194 45.63 -142.61
REMARK 500 GLN I 31 -112.13 55.70
REMARK 500 ARG I 97 48.59 -105.58
REMARK 500 ASP I 192 30.22 -145.74
REMARK 500 GLN I 203 47.69 -103.99
REMARK 500 ASP J 2 -95.15 -104.23
REMARK 500 VAL J 9 -166.76 -109.54
REMARK 500 SER J 31 33.47 -145.97
REMARK 500 ASP L 32 -115.59 50.03
REMARK 500 PHE L 103 69.12 -158.51
REMARK 500 ASN L 165 77.22 53.62
REMARK 500 ASP L 200 -65.13 67.62
REMARK 500 ILE M 5 -80.64 -104.64
REMARK 500 THR M 9 -150.42 -90.20
REMARK 500 ALA M 83 -113.46 -145.30
REMARK 500 LYS N 107 -144.89 58.62
REMARK 500 THR O 2 139.93 61.67
REMARK 500 TYR O 97 -65.95 -146.69
REMARK 500 ALA O 249 48.35 -96.31
REMARK 500 ARG P 8 75.04 56.48
REMARK 500 THR P 10 51.43 -117.81
REMARK 500 VAL P 51 91.43 -5.22
REMARK 500 ASN P 220 100.15 -53.96
REMARK 500 ASP P 221 -178.30 71.29
REMARK 500 PRO Q 183 108.65 -48.25
REMARK 500 GLN Q 202 -96.99 114.39
REMARK 500 ALA Q 205 -105.27 -82.16
REMARK 500 ARG R 45 75.40 58.02
REMARK 500 SER S 39 -154.17 -108.62
REMARK 500 ASP S 137 -158.94 -124.03
REMARK 500 ASP S 202 -61.09 67.37
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 78.7
REMARK 620 3 ARG G 122 O 75.5 71.1
REMARK 620 4 MET G 125 O 154.0 80.7 83.0
REMARK 620 N 1 2 3
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 104.0
REMARK 620 3 ASP Y 168 O 159.0 93.4
REMARK 620 4 SER Y 171 O 95.0 81.5 75.8
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 69.9
REMARK 620 3 SER N 169 O 93.1 69.2
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 92.7
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 J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO2 b 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
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: 4QVL 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 4QW3 A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QW3 B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QW3 C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QW3 D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QW3 E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QW3 F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QW3 G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QW3 H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QW3 I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QW3 J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QW3 K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QW3 L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QW3 M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QW3 N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QW3 O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QW3 P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QW3 Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QW3 R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QW3 S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QW3 T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QW3 U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QW3 V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QW3 W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QW3 X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QW3 Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QW3 Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QW3 a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QW3 b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQADV 4QW3 PHE K 63 UNP P30656 CYS 138 ENGINEERED MUTATION
SEQADV 4QW3 PHE Y 63 UNP P30656 CYS 138 ENGINEERED MUTATION
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 PHE 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 PHE 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 J 201 1
HET BO2 K 301 28
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 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 5(MG 2+)
FORMUL 30 CL 4(CL 1-)
FORMUL 31 BO2 6(C19 H25 B N4 O4)
FORMUL 44 HOH *253(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 GLU A 198 1 15
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 GLY D 26 1 14
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 SER M 105 1 18
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 LYS N 90 LEU N 93 5 4
HELIX 83 83 GLY N 128 PHE N 133 5 6
HELIX 84 84 ILE N 134 PHE N 142 1 9
HELIX 85 85 SER N 147 ASP N 166 1 20
HELIX 86 86 TYR N 189 GLU N 194 1 6
HELIX 87 87 LEU O 18 GLY O 31 1 14
HELIX 88 88 MET O 78 SER O 96 1 19
HELIX 89 89 TYR O 97 GLY O 102 1 6
HELIX 90 90 PRO O 106 ALA O 121 1 16
HELIX 91 91 GLY O 167 TRP O 179 1 13
HELIX 92 92 GLU O 184 GLU O 198 1 15
HELIX 93 93 ASN O 218 LEU O 222 5 5
HELIX 94 94 THR O 239 ALA O 249 1 11
HELIX 95 95 GLY P 1 ASP P 6 5 6
HELIX 96 96 LEU P 18 SER P 29 1 12
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 GLY R 26 1 14
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 6 ALA A 56 MET A 57 0
SHEET 2 B 6 TYR G 154 TYR G 157 -1 O GLY G 156 N MET A 57
SHEET 3 B 6 GLY G 142 THR G 148 -1 N ILE G 145 O TYR G 157
SHEET 4 B 6 ILE G 131 ASP G 138 -1 N PHE G 134 O TYR G 146
SHEET 5 B 6 GLY G 71 ASN G 75 -1 N GLY G 71 O VAL G 135
SHEET 6 B 6 ILE G 63 CYS G 65 -1 N PHE G 64 O MET G 72
SHEET 1 C 5 SER A 65 THR A 68 0
SHEET 2 C 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 C 5 VAL A 132 ASP A 140 -1 O LEU A 135 N VAL A 74
SHEET 4 C 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 C 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 D 6 TYR A 224 THR A 225 0
SHEET 2 D 6 ALA H 184 LEU H 191 1 O ALA H 184 N THR A 225
SHEET 3 D 6 VAL H 173 GLU H 179 -1 N VAL H 177 O GLU H 185
SHEET 4 D 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 D 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 D 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 E 5 ALA B 161 VAL B 164 0
SHEET 2 E 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 E 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 E 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 E 5 TYR B 225 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 F 5 LEU B 65 LYS B 67 0
SHEET 2 F 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 F 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 F 5 GLY B 144 SER B 150 -1 O GLN B 146 N GLY B 138
SHEET 5 F 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 G 5 ALA C 159 ILE C 162 0
SHEET 2 G 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 G 5 VAL C 40 GLU C 45 -1 O VAL C 41 N VAL C 34
SHEET 4 G 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 G 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 H 5 SER C 63 ASP C 66 0
SHEET 2 H 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 H 5 VAL C 129 PHE C 136 -1 O ALA C 134 N VAL C 70
SHEET 4 H 5 PRO C 143 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 H 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 I 5 ALA D 161 ILE D 164 0
SHEET 2 I 5 ALA D 29 ALA D 33 -1 N GLY D 31 O LYS D 162
SHEET 3 I 5 VAL D 38 GLU D 43 -1 O VAL D 39 N ILE D 32
SHEET 4 I 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 I 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 J 5 ILE D 59 ASP D 63 0
SHEET 2 J 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 J 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 J 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 J 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 K 5 GLY E 157 ILE E 160 0
SHEET 2 K 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 K 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 K 5 LEU E 210 GLY E 216 -1 O ALA E 213 N LEU E 45
SHEET 5 K 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 L 5 ILE E 62 ASP E 66 0
SHEET 2 L 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 L 5 VAL E 129 ASP E 137 -1 O LEU E 132 N SER E 72
SHEET 4 L 5 GLY E 140 PHE E 146 -1 O LEU E 144 N ILE E 133
SHEET 5 L 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 M 5 GLY F 158 THR F 161 0
SHEET 2 M 5 SER F 33 CYS F 38 -1 N GLY F 35 O ALA F 159
SHEET 3 M 5 GLY F 41 LEU F 49 -1 O GLY F 41 N CYS F 38
SHEET 4 M 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 M 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 N 5 GLN F 64 VAL F 66 0
SHEET 2 N 5 ILE F 70 GLY F 76 -1 O ILE F 70 N VAL F 66
SHEET 3 N 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 N 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 N 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 O 5 ALA G 159 THR G 162 0
SHEET 2 O 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 O 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 O 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 O 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
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 ILE H 99 N ALA H 44
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 ILE I 22 O TYR I 187
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 VAL J 13 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 U 5 VAL J 179 ASP J 185 -1 O ILE J 180 N SER J 17
SHEET 5 U 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 V 2 VAL J 21 ARG J 23 0
SHEET 2 V 2 SER J 26 LYS J 29 -1 O LYS J 29 N VAL J 21
SHEET 1 W 5 THR J 35 SER J 39 0
SHEET 2 W 5 THR J 42 GLY J 48 -1 O MET J 44 N ARG J 36
SHEET 3 W 5 VAL J 100 ASP J 108 -1 O GLY J 105 N LEU J 43
SHEET 4 W 5 LYS J 113 ILE J 119 -1 O 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 GLY K 184 N THR K 181
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 42 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 PHE L 44 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 PHE L 125 N THR L 109
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 PRO M 44 -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 TYR M 137 -1 O TYR M 137 N TYR M 129
SHEET 1 AF 5 THR M 141 ALA M 143 0
SHEET 2 AF 5 VAL M 11 TYR M 16 -1 N SER M 13 O LEU M 142
SHEET 3 AF 5 GLY M 19 ASP M 25 -1 O ALA M 23 N ILE M 12
SHEET 4 AF 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AF 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 PHE N 8 -1 N 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 VAL N 183 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 LEU O 135 N VAL O 74
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 ALA V 184 N THR O 225
SHEET 3 AM 6 VAL V 173 GLU V 179 -1 N VAL V 177 O GLU V 185
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 125 N GLY V 5
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 GLN P 146 N GLY P 138
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 VAL Q 41 N VAL Q 34
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 ASP Q 66 0
SHEET 2 AQ 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AQ 5 VAL Q 129 PHE Q 136 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AQ 5 PRO Q 143 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AQ 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AR 5 ALA R 161 ILE R 164 0
SHEET 2 AR 5 ALA R 29 ALA R 33 -1 N GLY R 31 O LYS R 162
SHEET 3 AR 5 VAL R 38 GLU R 43 -1 O VAL R 39 N ILE R 32
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 LEU S 71 N ILE S 63
SHEET 3 AU 5 VAL S 129 ASP S 137 -1 O LEU S 132 N SER S 72
SHEET 4 AU 5 GLY S 140 PHE S 146 -1 O LEU S 144 N ILE S 133
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 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AV 5 GLY T 41 LEU T 49 -1 O GLY T 41 N CYS T 38
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 ILE T 70 N VAL T 66
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 ILE V 99 N ALA V 44
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 ILE W 22 O TYR W 187
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 VAL X 13 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O ILE X 180 N SER X 17
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 BE 2 VAL X 21 ARG X 23 0
SHEET 2 BE 2 SER X 26 LYS X 29 -1 O 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 MET X 44 N ARG X 36
SHEET 3 BF 5 VAL X 100 ASP X 108 -1 O GLY X 105 N LEU X 43
SHEET 4 BF 5 LYS X 113 ILE X 119 -1 O GLU X 115 N GLY X 106
SHEET 5 BF 5 LYS X 125 GLU X 127 -1 O VAL X 126 N GLN X 118
SHEET 1 BG 5 ILE Y 126 VAL Y 129 0
SHEET 2 BG 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O 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 GLY Y 184 N THR Y 181
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 BI 5 VAL Y 34 GLU Y 36 0
SHEET 2 BI 5 LEU Y 42 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BI 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BI 5 GLY Y 109 ASP Y 116 -1 O VAL Y 115 N THR Y 99
SHEET 5 BI 5 ARG Y 121 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 PHE Z 44 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 PHE Z 125 N THR Z 109
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 TYR a 137 -1 O TYR a 137 N TYR a 129
SHEET 1 BO 5 THR a 141 ALA a 143 0
SHEET 2 BO 5 VAL a 11 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 VAL b 183 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 LEU b 122 N VAL b 110
LINK OG1 THR H 1 B26 BO2 H 301 1555 1555 1.43
LINK OG1 THR K 1 B26 BO2 K 301 1555 1555 1.43
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 1.44
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.52
LINK O TYR G 119 MG MG G 301 1555 1555 2.91
LINK O ARG G 122 MG MG G 301 1555 1555 2.71
LINK O MET G 125 MG MG G 301 1555 1555 2.26
LINK O ASP I 204 MG MG Y 302 1555 1555 2.35
LINK O ILE N 163 MG MG N 202 1555 1555 2.71
LINK O ASP N 166 MG MG N 202 1555 1555 2.82
LINK O SER N 169 MG MG N 202 1555 1555 2.58
LINK O ALA Y 165 MG MG Y 302 1555 1555 2.40
LINK O ASP Y 168 MG MG Y 302 1555 1555 2.27
LINK O SER Y 171 MG MG Y 302 1555 1555 2.86
LINK O THR Z 192 MG MG Z 301 1555 1555 2.92
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.46
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 10 THR H 1 SER H 20 THR H 21 GLN H 22
SITE 2 AC3 10 GLY H 45 GLY H 47 ALA H 49 THR H 52
SITE 3 AC3 10 GLY H 168 ASP I 124
SITE 1 AC4 2 GLN J 118 THR J 124
SITE 1 AC5 8 THR K 1 ALA K 20 THR K 21 LYS K 33
SITE 2 AC5 8 MET K 45 GLY K 47 ALA K 49 ASP L 126
SITE 1 AC6 9 HIS H 114 SER H 118 THR N 1 THR N 20
SITE 2 AC6 9 THR N 21 THR N 22 ARG N 45 GLY N 47
SITE 3 AC6 9 ALA N 49
SITE 1 AC7 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC7 5 LEU a 34
SITE 1 AC8 2 ARG N 45 GLN N 53
SITE 1 AC9 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 BC1 9 THR V 1 SER V 20 THR V 21 GLN V 22
SITE 2 BC1 9 GLY V 45 GLY V 47 ALA V 49 THR V 52
SITE 3 BC1 9 GLY V 168
SITE 1 BC2 8 THR Y 1 ALA Y 20 THR Y 21 LYS Y 33
SITE 2 BC2 8 MET Y 45 GLY Y 47 ALA Y 49 ASP Z 126
SITE 1 BC3 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 BC3 5 SER Y 171
SITE 1 BC4 5 ARG Z 28 THR Z 192 HIS Z 195 VAL Z 198
SITE 2 BC4 5 ASP Z 222
SITE 1 BC5 9 HIS V 114 SER V 118 THR b 1 THR b 20
SITE 2 BC5 9 THR b 21 THR b 22 ARG b 45 GLY b 47
SITE 3 BC5 9 ALA b 49
SITE 1 BC6 2 ARG b 45 GLN b 53
CRYST1 138.140 299.960 146.570 90.00 113.18 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 0.007239 0.000000 0.003099 0.00000
SCALE2 0.000000 0.003334 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007422 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 -0.999686 -0.000676 0.025029 69.26772 1
MTRIX2 2 -0.003696 -0.984702 -0.174205 -288.34915 1
MTRIX3 2 0.024764 -0.174243 0.984391 -26.05096 1
(ATOM LINES ARE NOT SHOWN.)
END
