HEADER HYDROLASE 23-DEC-15 5H8K
TITLE CRYSTAL STRUCTURE OF MEDICAGO TRUNCATULA N-CARBAMOYLPUTRESCINE
TITLE 2 AMIDOHYDROLASE (MTCPA) C158S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-CARBAMOYLPUTRESCINE AMIDOHYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEDICAGO TRUNCATULA;
SOURCE 3 ORGANISM_COMMON: BARREL MEDIC;
SOURCE 4 ORGANISM_TAXID: 3880;
SOURCE 5 GENE: MTR_2G086600;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD (DE3)
KEYWDS AMIDASE, HELICAL OCTAMER, ALPHA-BETA-BETA-ALPHA SANDWICH FOLD,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SEKULA,M.RUSZKOWSKI,M.MALINSKA,Z.DAUTER
REVDAT 2 27-SEP-23 5H8K 1 REMARK
REVDAT 1 20-APR-16 5H8K 0
JRNL AUTH B.SEKULA,M.RUSZKOWSKI,M.MALINSKA,Z.DAUTER
JRNL TITL STRUCTURAL INVESTIGATIONS OF N-CARBAMOYLPUTRESCINE
JRNL TITL 2 AMIDOHYDROLASE FROM MEDICAGO TRUNCATULA: INSIGHTS INTO THE
JRNL TITL 3 ULTIMATE STEP OF PUTRESCINE BIOSYNTHESIS IN PLANTS.
JRNL REF FRONT PLANT SCI V. 7 350 2016
JRNL REFN ESSN 1664-462X
JRNL PMID 27066023
JRNL DOI 10.3389/FPLS.2016.00350
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 258839
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2615
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17992
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 182
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 37528
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 310
REMARK 3 SOLVENT ATOMS : 3009
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.10000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 1.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.249
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.172
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.166
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 38718 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 36841 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 52309 ; 1.690 ; 1.889
REMARK 3 BOND ANGLES OTHERS (DEGREES): 84716 ; 0.809 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4728 ; 7.229 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1882 ;40.053 ;24.081
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6497 ;15.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 240 ;18.808 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5632 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 43933 ; 0.020 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 9151 ; 0.016 ; 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): 18912 ; 1.435 ; 1.440
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 18911 ; 1.434 ; 1.440
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23604 ; 2.268 ; 2.150
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 23605 ; 2.268 ; 2.150
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 19806 ; 2.344 ; 1.686
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 19806 ; 2.344 ; 1.686
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 28694 ; 3.395 ; 2.413
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 45219 ; 9.182 ;13.411
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 45220 ; 9.182 ;13.412
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 303
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3230 92.1630 -13.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.4487 T22: 0.5465
REMARK 3 T33: 0.2406 T12: 0.0372
REMARK 3 T13: -0.0398 T23: -0.2365
REMARK 3 L TENSOR
REMARK 3 L11: 1.5722 L22: 2.6667
REMARK 3 L33: 2.2978 L12: -0.0480
REMARK 3 L13: -0.3586 L23: 1.3863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: -0.5209 S13: 0.1779
REMARK 3 S21: 0.4407 S22: 0.0219 S23: -0.0832
REMARK 3 S31: -0.0903 S32: 0.0054 S33: 0.0257
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 303
REMARK 3 ORIGIN FOR THE GROUP (A): 57.7640 74.4500 -34.3070
REMARK 3 T TENSOR
REMARK 3 T11: 0.3430 T22: 0.3342
REMARK 3 T33: 0.1619 T12: -0.0048
REMARK 3 T13: 0.0337 T23: -0.0605
REMARK 3 L TENSOR
REMARK 3 L11: 2.2674 L22: 1.4607
REMARK 3 L33: 1.1613 L12: 0.0391
REMARK 3 L13: 0.1802 L23: 0.3576
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: -0.2857 S13: 0.1550
REMARK 3 S21: 0.0071 S22: 0.0345 S23: -0.3266
REMARK 3 S31: -0.0130 S32: 0.1680 S33: 0.0132
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 303
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6180 74.0150 -53.9610
REMARK 3 T TENSOR
REMARK 3 T11: 0.4502 T22: 0.2524
REMARK 3 T33: 0.1129 T12: 0.0447
REMARK 3 T13: -0.0833 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.9188 L22: 2.4253
REMARK 3 L33: 1.1793 L12: 0.0564
REMARK 3 L13: 0.1014 L23: 0.0341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0855 S12: -0.0311 S13: 0.2535
REMARK 3 S21: -0.4010 S22: 0.0313 S23: 0.3300
REMARK 3 S31: -0.1503 S32: -0.1003 S33: 0.0542
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 303
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7830 43.6980 -61.2650
REMARK 3 T TENSOR
REMARK 3 T11: 0.5236 T22: 0.2772
REMARK 3 T33: 0.0282 T12: 0.0414
REMARK 3 T13: 0.0241 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.9380 L22: 2.2706
REMARK 3 L33: 1.0567 L12: 0.2996
REMARK 3 L13: 0.0430 L23: 0.2752
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.0946 S13: -0.1547
REMARK 3 S21: -0.4993 S22: 0.0613 S23: -0.1218
REMARK 3 S31: 0.0663 S32: 0.0776 S33: -0.0243
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 303
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7640 34.9970 -32.4950
REMARK 3 T TENSOR
REMARK 3 T11: 0.3746 T22: 0.3816
REMARK 3 T33: 0.1056 T12: -0.0516
REMARK 3 T13: -0.0089 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 1.6401 L22: 1.6324
REMARK 3 L33: 1.2134 L12: 0.0349
REMARK 3 L13: 0.2244 L23: -0.1724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0744 S12: -0.3155 S13: -0.1325
REMARK 3 S21: 0.1268 S22: -0.1156 S23: 0.3166
REMARK 3 S31: 0.0489 S32: -0.1681 S33: 0.0412
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 303
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2340 12.9640 -26.2110
REMARK 3 T TENSOR
REMARK 3 T11: 0.4908 T22: 0.4255
REMARK 3 T33: 0.3316 T12: -0.0312
REMARK 3 T13: -0.0783 T23: 0.2281
REMARK 3 L TENSOR
REMARK 3 L11: 1.5992 L22: 2.4280
REMARK 3 L33: 1.3928 L12: -0.0655
REMARK 3 L13: 0.2418 L23: -1.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.1571 S12: -0.3043 S13: -0.4882
REMARK 3 S21: 0.1456 S22: -0.1940 S23: -0.2526
REMARK 3 S31: 0.2710 S32: 0.1522 S33: 0.0369
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 303
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6900 40.6420 -0.2490
REMARK 3 T TENSOR
REMARK 3 T11: 1.0623 T22: 1.0506
REMARK 3 T33: 0.2712 T12: -0.3435
REMARK 3 T13: -0.2204 T23: 0.2271
REMARK 3 L TENSOR
REMARK 3 L11: 1.4891 L22: 1.7364
REMARK 3 L33: 1.7516 L12: 0.1500
REMARK 3 L13: 0.0980 L23: 0.1231
REMARK 3 S TENSOR
REMARK 3 S11: 0.2612 S12: -0.6616 S13: 0.0552
REMARK 3 S21: 0.5942 S22: -0.2779 S23: -0.3977
REMARK 3 S31: -0.3125 S32: 0.2427 S33: 0.0167
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 303
REMARK 3 ORIGIN FOR THE GROUP (A): 74.2790 29.3270 -8.9050
REMARK 3 T TENSOR
REMARK 3 T11: 0.8847 T22: 1.4209
REMARK 3 T33: 1.1506 T12: -0.2181
REMARK 3 T13: -0.3592 T23: 0.4741
REMARK 3 L TENSOR
REMARK 3 L11: 3.1318 L22: 0.8238
REMARK 3 L33: 1.2547 L12: 0.4199
REMARK 3 L13: 0.2749 L23: 0.8572
REMARK 3 S TENSOR
REMARK 3 S11: 0.2140 S12: -0.3614 S13: -0.1566
REMARK 3 S21: 0.0837 S22: 0.1230 S23: -0.7115
REMARK 3 S31: 0.0231 S32: 0.6454 S33: -0.3370
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 303
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6360 88.0720 90.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.4569 T22: 0.3078
REMARK 3 T33: 0.1441 T12: -0.0257
REMARK 3 T13: 0.0594 T23: -0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 1.5943 L22: 2.5241
REMARK 3 L33: 2.6080 L12: -0.1128
REMARK 3 L13: -0.5636 L23: 1.8363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: -0.2606 S13: 0.0572
REMARK 3 S21: 0.2797 S22: 0.0317 S23: -0.0069
REMARK 3 S31: -0.1215 S32: 0.0716 S33: -0.0389
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 303
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0170 70.0900 69.9720
REMARK 3 T TENSOR
REMARK 3 T11: 0.3986 T22: 0.2862
REMARK 3 T33: 0.0962 T12: -0.0474
REMARK 3 T13: 0.0746 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 1.9761 L22: 1.4086
REMARK 3 L33: 1.1124 L12: 0.1527
REMARK 3 L13: -0.2096 L23: 0.2320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.0986 S13: 0.0873
REMARK 3 S21: -0.0088 S22: 0.0511 S23: -0.2586
REMARK 3 S31: -0.0475 S32: 0.2144 S33: -0.0302
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 303
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8030 69.7650 50.2380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5003 T22: 0.2986
REMARK 3 T33: 0.0853 T12: 0.0441
REMARK 3 T13: -0.0455 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.8586 L22: 2.4298
REMARK 3 L33: 1.1019 L12: 0.1168
REMARK 3 L13: 0.0478 L23: 0.0240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0253 S12: 0.1550 S13: 0.1910
REMARK 3 S21: -0.3742 S22: 0.0320 S23: 0.3432
REMARK 3 S31: -0.2417 S32: -0.0698 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 303
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7080 39.2860 43.1680
REMARK 3 T TENSOR
REMARK 3 T11: 0.4733 T22: 0.3304
REMARK 3 T33: 0.0184 T12: -0.0037
REMARK 3 T13: 0.0201 T23: -0.0514
REMARK 3 L TENSOR
REMARK 3 L11: 0.7414 L22: 2.0920
REMARK 3 L33: 1.1736 L12: 0.3322
REMARK 3 L13: 0.0771 L23: 0.2129
REMARK 3 S TENSOR
REMARK 3 S11: -0.0722 S12: 0.1945 S13: -0.1095
REMARK 3 S21: -0.4568 S22: 0.1032 S23: -0.0641
REMARK 3 S31: -0.0113 S32: 0.0921 S33: -0.0310
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 303
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3750 30.9300 71.7960
REMARK 3 T TENSOR
REMARK 3 T11: 0.3517 T22: 0.2848
REMARK 3 T33: 0.1994 T12: 0.0019
REMARK 3 T13: 0.0534 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.4071 L22: 1.4989
REMARK 3 L33: 1.1697 L12: -0.3467
REMARK 3 L13: 0.4316 L23: -0.1868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: -0.1216 S13: -0.1242
REMARK 3 S21: 0.1459 S22: 0.0615 S23: 0.4765
REMARK 3 S31: 0.0026 S32: -0.1810 S33: -0.0090
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 303
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6750 8.8600 78.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.4134 T22: 0.2530
REMARK 3 T33: 0.1424 T12: 0.0110
REMARK 3 T13: 0.0225 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.3274 L22: 1.7817
REMARK 3 L33: 1.2182 L12: -0.2535
REMARK 3 L13: 0.4148 L23: -0.7378
REMARK 3 S TENSOR
REMARK 3 S11: 0.0583 S12: -0.0390 S13: -0.2861
REMARK 3 S21: 0.1607 S22: 0.0256 S23: 0.0995
REMARK 3 S31: 0.1401 S32: 0.0398 S33: -0.0839
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 303
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9060 36.8280 104.4670
REMARK 3 T TENSOR
REMARK 3 T11: 0.9087 T22: 0.4203
REMARK 3 T33: 0.1092 T12: 0.0263
REMARK 3 T13: -0.0997 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.6542 L22: 1.4190
REMARK 3 L33: 1.5858 L12: -0.3547
REMARK 3 L13: 0.0335 L23: 0.2746
REMARK 3 S TENSOR
REMARK 3 S11: -0.1459 S12: -0.2573 S13: 0.1989
REMARK 3 S21: 0.6066 S22: 0.1042 S23: -0.1502
REMARK 3 S31: -0.3071 S32: 0.0716 S33: 0.0417
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 303
REMARK 3 ORIGIN FOR THE GROUP (A): 73.7710 25.8920 96.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.7054 T22: 0.6662
REMARK 3 T33: 0.5322 T12: -0.0687
REMARK 3 T13: -0.3216 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 4.1277 L22: 1.1055
REMARK 3 L33: 1.5629 L12: -0.8305
REMARK 3 L13: 0.3471 L23: 0.6032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: -0.0328 S13: 0.2196
REMARK 3 S21: 0.3135 S22: 0.0985 S23: -0.6500
REMARK 3 S31: -0.1677 S32: 0.5182 S33: -0.0555
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 5H8K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 261455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.17
REMARK 200 R MERGE FOR SHELL (I) : 0.73800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 1ERZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 8% TACSIMATE AT PH 7.0,
REMARK 280 10% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 76.26550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 105.37800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.26550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 105.37800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 40720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 39530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -151.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, M, N, O, P
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 ASP A 4
REMARK 465 HIS A 189
REMARK 465 ASP A 190
REMARK 465 GLN A 191
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 ASP B 4
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 SER E -2
REMARK 465 ASN E -1
REMARK 465 ALA E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 ASP E 4
REMARK 465 SER F -2
REMARK 465 ASN F -1
REMARK 465 ALA F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 SER G -2
REMARK 465 ASN G -1
REMARK 465 ALA G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 GLU G 3
REMARK 465 ASP G 4
REMARK 465 LYS G 5
REMARK 465 GLY G 6
REMARK 465 SER H -2
REMARK 465 ASN H -1
REMARK 465 ALA H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLU H 3
REMARK 465 ASP H 4
REMARK 465 ASP H 126
REMARK 465 GLY H 127
REMARK 465 PRO H 128
REMARK 465 GLY H 129
REMARK 465 GLU H 187
REMARK 465 PRO H 188
REMARK 465 HIS H 189
REMARK 465 ASP H 190
REMARK 465 GLN H 191
REMARK 465 SER H 192
REMARK 465 ILE H 193
REMARK 465 THR H 227
REMARK 465 GLU H 228
REMARK 465 HIS H 229
REMARK 465 GLY H 230
REMARK 465 LYS H 231
REMARK 465 SER H 232
REMARK 465 GLU H 233
REMARK 465 LEU H 301
REMARK 465 SER I -2
REMARK 465 ASN I -1
REMARK 465 ALA I 0
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 GLU I 3
REMARK 465 HIS I 189
REMARK 465 ASP I 190
REMARK 465 GLN I 191
REMARK 465 SER I 192
REMARK 465 ILE I 193
REMARK 465 SER J -2
REMARK 465 ASN J -1
REMARK 465 ALA J 0
REMARK 465 MET J 1
REMARK 465 ALA J 2
REMARK 465 GLU J 3
REMARK 465 SER K -2
REMARK 465 ASN K -1
REMARK 465 ALA K 0
REMARK 465 SER L -2
REMARK 465 ASN L -1
REMARK 465 ALA L 0
REMARK 465 MET L 1
REMARK 465 ALA L 2
REMARK 465 GLU L 3
REMARK 465 SER M -2
REMARK 465 ASN M -1
REMARK 465 ALA M 0
REMARK 465 MET M 1
REMARK 465 ALA M 2
REMARK 465 GLU M 3
REMARK 465 ASP M 4
REMARK 465 SER N -2
REMARK 465 ASN N -1
REMARK 465 ALA N 0
REMARK 465 MET N 1
REMARK 465 ALA N 2
REMARK 465 GLU N 3
REMARK 465 SER O -2
REMARK 465 ASN O -1
REMARK 465 ALA O 0
REMARK 465 MET O 1
REMARK 465 ALA O 2
REMARK 465 GLU O 3
REMARK 465 ASP O 4
REMARK 465 SER P -2
REMARK 465 ASN P -1
REMARK 465 ALA P 0
REMARK 465 MET P 1
REMARK 465 ALA P 2
REMARK 465 GLU P 3
REMARK 465 PRO P 128
REMARK 465 GLY P 129
REMARK 465 HIS P 189
REMARK 465 ASP P 190
REMARK 465 GLN P 191
REMARK 465 SER P 192
REMARK 465 GLU P 228
REMARK 465 HIS P 229
REMARK 465 GLY P 230
REMARK 465 LEU P 301
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS L 276 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 99 57.99 71.99
REMARK 500 ASP A 126 43.77 -84.57
REMARK 500 SER A 158 -116.39 38.36
REMARK 500 ASN A 239 28.49 49.05
REMARK 500 LYS A 256 -8.79 -152.29
REMARK 500 LYS A 297 -50.92 -139.30
REMARK 500 ASN B 99 -114.23 49.46
REMARK 500 GLU B 131 48.86 -75.38
REMARK 500 SER B 158 -108.86 50.75
REMARK 500 LYS B 256 -7.09 -150.57
REMARK 500 ARG B 284 76.80 -118.25
REMARK 500 LYS B 297 -50.39 -138.02
REMARK 500 ASN C 99 -109.91 49.27
REMARK 500 TYR C 130 56.81 -140.62
REMARK 500 GLU C 131 48.96 -87.37
REMARK 500 SER C 158 -110.75 45.61
REMARK 500 LYS C 256 -25.01 -148.36
REMARK 500 LYS C 297 -43.67 -137.69
REMARK 500 TYR D 54 91.52 -69.52
REMARK 500 CYS D 56 8.01 -68.08
REMARK 500 ASN D 99 -113.61 55.67
REMARK 500 TYR D 130 56.95 -140.17
REMARK 500 SER D 158 -116.74 50.71
REMARK 500 LYS D 256 -18.74 -143.63
REMARK 500 LYS D 297 -46.42 -133.50
REMARK 500 ASN E 99 -126.91 53.06
REMARK 500 SER E 158 -118.48 47.07
REMARK 500 SER E 186 173.19 -57.48
REMARK 500 LYS E 256 -20.13 -140.79
REMARK 500 LYS E 297 -47.88 -140.72
REMARK 500 PHE F 50 -7.89 -58.82
REMARK 500 ASN F 99 -124.14 58.41
REMARK 500 TYR F 130 56.15 -144.75
REMARK 500 GLU F 131 37.75 -81.79
REMARK 500 ALA F 151 157.49 179.61
REMARK 500 SER F 158 -116.23 42.73
REMARK 500 ASP F 190 91.36 -165.57
REMARK 500 LYS F 256 -23.13 -149.43
REMARK 500 LYS F 297 -52.14 -143.17
REMARK 500 LYS G 8 75.85 -109.12
REMARK 500 ASP G 20 30.01 -96.41
REMARK 500 TYR G 54 98.83 -63.55
REMARK 500 CYS G 56 6.56 -67.97
REMARK 500 GLN G 65 7.02 -69.90
REMARK 500 ASN G 99 -115.73 55.71
REMARK 500 THR G 114 119.05 -36.00
REMARK 500 LYS G 121 120.32 -29.70
REMARK 500 GLU G 131 49.30 -82.95
REMARK 500 ALA G 151 159.24 178.29
REMARK 500 SER G 158 -114.54 44.63
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 719 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH C 756 DISTANCE = 6.32 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG G 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL I 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL I 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO I 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL J 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG J 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL K 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL K 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO K 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG L 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL M 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL M 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL M 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL N 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL N 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL N 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL N 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL O 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL P 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H8I RELATED DB: PDB
REMARK 900 RELATED ID: 5H8J RELATED DB: PDB
REMARK 900 RELATED ID: 5H8L RELATED DB: PDB
DBREF 5H8K A 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K B 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K C 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K D 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K E 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K F 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K G 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K H 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K I 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K J 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K K 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K L 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K M 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K N 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K O 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
DBREF 5H8K P 1 301 UNP G7ITU5 G7ITU5_MEDTR 1 301
SEQADV 5H8K SER A -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN A -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA A 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER A 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER B -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN B -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA B 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER B 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER C -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN C -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA C 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER C 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER D -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN D -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA D 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER D 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER E -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN E -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA E 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER E 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER F -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN F -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA F 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER F 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER G -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN G -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA G 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER G 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER H -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN H -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA H 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER H 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER I -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN I -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA I 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER I 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER J -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN J -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA J 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER J 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER K -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN K -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA K 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER K 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER L -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN L -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA L 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER L 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER M -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN M -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA M 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER M 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER N -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN N -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA N 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER N 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER O -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN O -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA O 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER O 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQADV 5H8K SER P -2 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ASN P -1 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K ALA P 0 UNP G7ITU5 EXPRESSION TAG
SEQADV 5H8K SER P 158 UNP G7ITU5 CYS 158 ENGINEERED MUTATION
SEQRES 1 A 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 A 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 A 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 A 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 A 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 A 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 A 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 A 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 A 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 A 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 A 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 A 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 A 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 A 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 A 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 A 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 A 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 A 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 A 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 A 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 A 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 A 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 A 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 A 304 LYS ASN PRO VAL LEU
SEQRES 1 B 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 B 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 B 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 B 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 B 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 B 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 B 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 B 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 B 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 B 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 B 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 B 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 B 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 B 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 B 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 B 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 B 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 B 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 B 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 B 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 B 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 B 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 B 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 B 304 LYS ASN PRO VAL LEU
SEQRES 1 C 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 C 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 C 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 C 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 C 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 C 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 C 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 C 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 C 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 C 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 C 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 C 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 C 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 C 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 C 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 C 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 C 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 C 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 C 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 C 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 C 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 C 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 C 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 C 304 LYS ASN PRO VAL LEU
SEQRES 1 D 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 D 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 D 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 D 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 D 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 D 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 D 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 D 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 D 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 D 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 D 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 D 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 D 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 D 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 D 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 D 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 D 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 D 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 D 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 D 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 D 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 D 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 D 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 D 304 LYS ASN PRO VAL LEU
SEQRES 1 E 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 E 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 E 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 E 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 E 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 E 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 E 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 E 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 E 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 E 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 E 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 E 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 E 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 E 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 E 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 E 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 E 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 E 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 E 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 E 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 E 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 E 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 E 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 E 304 LYS ASN PRO VAL LEU
SEQRES 1 F 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 F 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 F 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 F 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 F 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 F 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 F 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 F 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 F 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 F 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 F 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 F 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 F 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 F 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 F 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 F 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 F 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 F 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 F 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 F 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 F 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 F 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 F 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 F 304 LYS ASN PRO VAL LEU
SEQRES 1 G 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 G 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 G 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 G 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 G 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 G 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 G 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 G 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 G 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 G 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 G 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 G 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 G 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 G 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 G 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 G 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 G 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 G 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 G 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 G 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 G 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 G 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 G 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 G 304 LYS ASN PRO VAL LEU
SEQRES 1 H 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 H 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 H 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 H 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 H 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 H 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 H 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 H 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 H 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 H 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 H 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 H 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 H 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 H 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 H 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 H 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 H 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 H 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 H 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 H 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 H 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 H 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 H 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 H 304 LYS ASN PRO VAL LEU
SEQRES 1 I 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 I 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 I 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 I 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 I 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 I 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 I 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 I 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 I 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 I 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 I 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 I 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 I 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 I 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 I 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 I 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 I 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 I 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 I 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 I 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 I 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 I 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 I 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 I 304 LYS ASN PRO VAL LEU
SEQRES 1 J 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 J 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 J 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 J 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 J 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 J 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 J 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 J 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 J 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 J 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 J 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 J 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 J 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 J 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 J 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 J 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 J 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 J 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 J 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 J 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 J 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 J 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 J 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 J 304 LYS ASN PRO VAL LEU
SEQRES 1 K 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 K 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 K 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 K 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 K 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 K 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 K 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 K 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 K 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 K 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 K 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 K 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 K 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 K 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 K 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 K 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 K 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 K 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 K 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 K 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 K 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 K 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 K 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 K 304 LYS ASN PRO VAL LEU
SEQRES 1 L 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 L 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 L 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 L 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 L 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 L 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 L 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 L 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 L 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 L 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 L 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 L 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 L 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 L 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 L 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 L 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 L 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 L 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 L 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 L 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 L 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 L 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 L 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 L 304 LYS ASN PRO VAL LEU
SEQRES 1 M 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 M 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 M 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 M 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 M 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 M 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 M 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 M 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 M 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 M 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 M 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 M 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 M 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 M 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 M 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 M 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 M 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 M 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 M 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 M 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 M 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 M 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 M 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 M 304 LYS ASN PRO VAL LEU
SEQRES 1 N 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 N 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 N 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 N 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 N 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 N 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 N 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 N 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 N 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 N 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 N 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 N 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 N 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 N 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 N 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 N 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 N 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 N 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 N 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 N 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 N 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 N 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 N 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 N 304 LYS ASN PRO VAL LEU
SEQRES 1 O 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 O 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 O 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 O 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 O 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 O 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 O 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 O 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 O 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 O 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 O 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 O 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 O 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 O 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 O 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 O 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 O 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 O 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 O 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 O 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 O 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 O 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 O 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 O 304 LYS ASN PRO VAL LEU
SEQRES 1 P 304 SER ASN ALA MET ALA GLU ASP LYS GLY ARG LYS VAL VAL
SEQRES 2 P 304 VAL SER ALA LEU GLN PHE ALA CYS THR ASP ASP VAL SER
SEQRES 3 P 304 THR ASN VAL THR THR ALA GLU ARG LEU VAL ARG ALA ALA
SEQRES 4 P 304 HIS LYS GLN GLY ALA ASN ILE VAL LEU ILE GLN GLU LEU
SEQRES 5 P 304 PHE GLU GLY TYR TYR PHE CYS GLN ALA GLN ARG GLU ASP
SEQRES 6 P 304 PHE ILE GLN ARG ALA LYS PRO TYR LYS ASP HIS PRO THR
SEQRES 7 P 304 ILE MET ARG LEU GLN LYS LEU ALA LYS GLU LEU GLY VAL
SEQRES 8 P 304 VAL ILE PRO VAL SER PHE PHE GLU GLU ALA ASN ASN ALA
SEQRES 9 P 304 HIS TYR ASN SER ILE ALA ILE ILE ASP ALA ASP GLY THR
SEQRES 10 P 304 ASP LEU GLY ILE TYR ARG LYS SER HIS ILE PRO ASP GLY
SEQRES 11 P 304 PRO GLY TYR GLU GLU LYS PHE TYR PHE ASN PRO GLY ASP
SEQRES 12 P 304 THR GLY PHE LYS VAL PHE GLN THR LYS TYR ALA LYS ILE
SEQRES 13 P 304 GLY VAL ALA ILE SER TRP ASP GLN TRP PHE PRO GLU ALA
SEQRES 14 P 304 ALA ARG ALA MET ALA LEU GLN GLY ALA GLU ILE LEU PHE
SEQRES 15 P 304 TYR PRO THR ALA ILE GLY SER GLU PRO HIS ASP GLN SER
SEQRES 16 P 304 ILE ASP SER ARG ASP HIS TRP LYS ARG VAL MET GLN GLY
SEQRES 17 P 304 HIS ALA GLY ALA ASN LEU VAL PRO LEU VAL ALA SER ASN
SEQRES 18 P 304 ARG ILE GLY ASN GLU ILE ILE GLU THR GLU HIS GLY LYS
SEQRES 19 P 304 SER GLU ILE LYS PHE TYR GLY ASN SER PHE ILE ALA GLY
SEQRES 20 P 304 PRO THR GLY GLU ILE VAL SER ILE ALA ASP ASP LYS GLU
SEQRES 21 P 304 GLU ALA VAL LEU ILE ALA GLU PHE ASN LEU ASP LYS ILE
SEQRES 22 P 304 LYS SER MET ARG HIS CYS TRP GLY VAL PHE ARG ASP ARG
SEQRES 23 P 304 ARG PRO ASP LEU TYR LYS VAL LEU LEU THR LEU ASP GLY
SEQRES 24 P 304 LYS ASN PRO VAL LEU
HET GOL A 401 6
HET GOL A 402 6
HET EDO A 403 4
HET GOL B 401 6
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET GOL B 405 6
HET GOL C 401 6
HET GOL C 402 6
HET GOL C 403 6
HET PEG C 404 7
HET EDO C 405 4
HET GOL D 401 6
HET GOL D 402 6
HET GOL D 403 6
HET GOL D 404 6
HET EDO D 405 4
HET GOL E 401 6
HET GOL E 402 6
HET GOL E 403 6
HET GOL E 404 6
HET GOL F 401 6
HET GOL F 402 6
HET GOL F 403 6
HET GOL G 401 6
HET GOL G 402 6
HET GOL G 403 6
HET PEG G 404 7
HET GOL I 401 6
HET GOL I 402 6
HET EDO I 403 4
HET GOL J 401 6
HET GOL J 402 6
HET PEG J 403 7
HET GOL K 401 6
HET GOL K 402 6
HET GOL K 403 6
HET EDO K 404 4
HET GOL L 401 6
HET GOL L 402 6
HET GOL L 403 6
HET PEG L 404 7
HET EDO L 405 4
HET GOL M 401 6
HET GOL M 402 6
HET GOL M 403 6
HET GOL N 401 6
HET GOL N 402 6
HET GOL N 403 6
HET GOL N 404 6
HET GOL O 401 6
HET GOL P 401 6
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 17 GOL 43(C3 H8 O3)
FORMUL 19 EDO 6(C2 H6 O2)
FORMUL 28 PEG 4(C4 H10 O3)
FORMUL 70 HOH *3009(H2 O)
HELIX 1 AA1 ASP A 21 GLN A 39 1 19
HELIX 2 AA2 GLU A 61 ALA A 67 5 7
HELIX 3 AA3 HIS A 73 GLY A 87 1 15
HELIX 4 AA4 GLU A 131 TYR A 135 5 5
HELIX 5 AA5 ILE A 157 TRP A 162 5 6
HELIX 6 AA6 PHE A 163 GLN A 173 1 11
HELIX 7 AA7 SER A 195 LEU A 211 1 17
HELIX 8 AA8 LEU A 267 GLY A 278 1 12
HELIX 9 AA9 GLY A 278 ARG A 283 1 6
HELIX 10 AB1 ARG A 284 THR A 293 5 10
HELIX 11 AB2 ASP B 21 GLN B 39 1 19
HELIX 12 AB3 TYR B 54 ALA B 58 5 5
HELIX 13 AB4 ARG B 60 GLN B 65 1 6
HELIX 14 AB5 HIS B 73 GLY B 87 1 15
HELIX 15 AB6 GLU B 131 TYR B 135 5 5
HELIX 16 AB7 ILE B 157 TRP B 162 5 6
HELIX 17 AB8 PHE B 163 GLN B 173 1 11
HELIX 18 AB9 SER B 195 LEU B 211 1 17
HELIX 19 AC1 LEU B 267 GLY B 278 1 12
HELIX 20 AC2 ARG B 284 THR B 293 5 10
HELIX 21 AC3 ASP C 21 GLN C 39 1 19
HELIX 22 AC4 TYR C 54 ALA C 58 5 5
HELIX 23 AC5 ARG C 60 GLN C 65 1 6
HELIX 24 AC6 HIS C 73 GLY C 87 1 15
HELIX 25 AC7 GLU C 131 TYR C 135 5 5
HELIX 26 AC8 ILE C 157 TRP C 162 5 6
HELIX 27 AC9 PHE C 163 GLN C 173 1 11
HELIX 28 AD1 SER C 195 LEU C 211 1 17
HELIX 29 AD2 LEU C 267 GLY C 278 1 12
HELIX 30 AD3 GLY C 278 ARG C 283 1 6
HELIX 31 AD4 ARG C 284 THR C 293 5 10
HELIX 32 AD5 ASP D 21 GLN D 39 1 19
HELIX 33 AD6 TYR D 54 ALA D 58 5 5
HELIX 34 AD7 ARG D 60 GLN D 65 1 6
HELIX 35 AD8 HIS D 73 GLY D 87 1 15
HELIX 36 AD9 GLU D 131 TYR D 135 5 5
HELIX 37 AE1 ILE D 157 TRP D 162 5 6
HELIX 38 AE2 PHE D 163 GLN D 173 1 11
HELIX 39 AE3 SER D 195 LEU D 211 1 17
HELIX 40 AE4 LEU D 267 GLY D 278 1 12
HELIX 41 AE5 GLY D 278 ARG D 283 1 6
HELIX 42 AE6 ARG D 284 THR D 293 5 10
HELIX 43 AE7 ASP E 21 GLN E 39 1 19
HELIX 44 AE8 TYR E 54 ALA E 58 5 5
HELIX 45 AE9 ARG E 60 GLN E 65 1 6
HELIX 46 AF1 HIS E 73 GLY E 87 1 15
HELIX 47 AF2 GLU E 131 TYR E 135 5 5
HELIX 48 AF3 ILE E 157 TRP E 162 5 6
HELIX 49 AF4 PHE E 163 GLN E 173 1 11
HELIX 50 AF5 SER E 195 LEU E 211 1 17
HELIX 51 AF6 LEU E 267 GLY E 278 1 12
HELIX 52 AF7 GLY E 278 ARG E 283 1 6
HELIX 53 AF8 ARG E 284 THR E 293 5 10
HELIX 54 AF9 ASP F 21 GLN F 39 1 19
HELIX 55 AG1 TYR F 54 ALA F 58 5 5
HELIX 56 AG2 ARG F 60 GLN F 65 1 6
HELIX 57 AG3 HIS F 73 GLY F 87 1 15
HELIX 58 AG4 GLU F 131 TYR F 135 5 5
HELIX 59 AG5 ILE F 157 TRP F 162 5 6
HELIX 60 AG6 PHE F 163 GLN F 173 1 11
HELIX 61 AG7 SER F 195 LEU F 211 1 17
HELIX 62 AG8 LEU F 267 GLY F 278 1 12
HELIX 63 AG9 GLY F 278 ARG F 283 1 6
HELIX 64 AH1 ARG F 284 THR F 293 5 10
HELIX 65 AH2 ASP G 21 GLN G 39 1 19
HELIX 66 AH3 TYR G 54 ALA G 58 5 5
HELIX 67 AH4 ARG G 60 GLN G 65 1 6
HELIX 68 AH5 HIS G 73 GLY G 87 1 15
HELIX 69 AH6 GLU G 131 TYR G 135 5 5
HELIX 70 AH7 ILE G 157 TRP G 162 5 6
HELIX 71 AH8 PHE G 163 GLN G 173 1 11
HELIX 72 AH9 SER G 195 LEU G 211 1 17
HELIX 73 AI1 LEU G 267 GLY G 278 1 12
HELIX 74 AI2 GLY G 278 ARG G 283 1 6
HELIX 75 AI3 ARG G 284 THR G 293 5 10
HELIX 76 AI4 ASP H 21 GLN H 39 1 19
HELIX 77 AI5 ARG H 60 ALA H 67 5 8
HELIX 78 AI6 HIS H 73 LYS H 84 1 12
HELIX 79 AI7 GLU H 131 TYR H 135 5 5
HELIX 80 AI8 ILE H 157 TRP H 162 5 6
HELIX 81 AI9 PHE H 163 GLN H 173 1 11
HELIX 82 AJ1 ARG H 196 LEU H 211 1 16
HELIX 83 AJ2 LEU H 267 GLY H 278 1 12
HELIX 84 AJ3 GLY H 278 ARG H 283 1 6
HELIX 85 AJ4 ARG H 284 THR H 293 5 10
HELIX 86 AJ5 ASP I 21 GLN I 39 1 19
HELIX 87 AJ6 ARG I 60 ALA I 67 5 8
HELIX 88 AJ7 HIS I 73 GLY I 87 1 15
HELIX 89 AJ8 GLU I 131 TYR I 135 5 5
HELIX 90 AJ9 ILE I 157 TRP I 162 5 6
HELIX 91 AK1 PHE I 163 LEU I 172 1 10
HELIX 92 AK2 SER I 195 LEU I 211 1 17
HELIX 93 AK3 LEU I 267 GLY I 278 1 12
HELIX 94 AK4 GLY I 278 ARG I 283 1 6
HELIX 95 AK5 ARG I 284 THR I 293 5 10
HELIX 96 AK6 ASP J 21 GLN J 39 1 19
HELIX 97 AK7 TYR J 54 ALA J 58 5 5
HELIX 98 AK8 ARG J 60 GLN J 65 1 6
HELIX 99 AK9 HIS J 73 GLY J 87 1 15
HELIX 100 AL1 GLU J 131 TYR J 135 5 5
HELIX 101 AL2 ILE J 157 TRP J 162 5 6
HELIX 102 AL3 PHE J 163 GLN J 173 1 11
HELIX 103 AL4 SER J 195 LEU J 211 1 17
HELIX 104 AL5 LEU J 267 GLY J 278 1 12
HELIX 105 AL6 GLY J 278 ARG J 283 1 6
HELIX 106 AL7 ARG J 284 THR J 293 5 10
HELIX 107 AL8 ASP K 21 GLN K 39 1 19
HELIX 108 AL9 TYR K 54 ALA K 58 5 5
HELIX 109 AM1 ARG K 60 GLN K 65 1 6
HELIX 110 AM2 HIS K 73 GLY K 87 1 15
HELIX 111 AM3 GLU K 131 TYR K 135 5 5
HELIX 112 AM4 ILE K 157 TRP K 162 5 6
HELIX 113 AM5 PHE K 163 GLN K 173 1 11
HELIX 114 AM6 SER K 195 LEU K 211 1 17
HELIX 115 AM7 LEU K 267 GLY K 278 1 12
HELIX 116 AM8 GLY K 278 ARG K 283 1 6
HELIX 117 AM9 ARG K 284 THR K 293 5 10
HELIX 118 AN1 ASP L 21 GLN L 39 1 19
HELIX 119 AN2 TYR L 54 ALA L 58 5 5
HELIX 120 AN3 ARG L 60 GLN L 65 1 6
HELIX 121 AN4 HIS L 73 GLY L 87 1 15
HELIX 122 AN5 GLU L 131 TYR L 135 5 5
HELIX 123 AN6 ILE L 157 TRP L 162 5 6
HELIX 124 AN7 PHE L 163 GLN L 173 1 11
HELIX 125 AN8 SER L 195 LEU L 211 1 17
HELIX 126 AN9 LEU L 267 GLY L 278 1 12
HELIX 127 AO1 GLY L 278 ARG L 283 1 6
HELIX 128 AO2 ARG L 284 THR L 293 5 10
HELIX 129 AO3 ASP M 21 GLN M 39 1 19
HELIX 130 AO4 TYR M 54 ALA M 58 5 5
HELIX 131 AO5 ARG M 60 GLN M 65 1 6
HELIX 132 AO6 HIS M 73 GLY M 87 1 15
HELIX 133 AO7 GLU M 131 TYR M 135 5 5
HELIX 134 AO8 ILE M 157 TRP M 162 5 6
HELIX 135 AO9 PHE M 163 GLN M 173 1 11
HELIX 136 AP1 SER M 195 LEU M 211 1 17
HELIX 137 AP2 LEU M 267 GLY M 278 1 12
HELIX 138 AP3 GLY M 278 ARG M 283 1 6
HELIX 139 AP4 ARG M 284 THR M 293 5 10
HELIX 140 AP5 ASP N 21 GLN N 39 1 19
HELIX 141 AP6 TYR N 54 ALA N 58 5 5
HELIX 142 AP7 ARG N 60 GLN N 65 1 6
HELIX 143 AP8 HIS N 73 GLY N 87 1 15
HELIX 144 AP9 GLU N 131 TYR N 135 5 5
HELIX 145 AQ1 ILE N 157 TRP N 162 5 6
HELIX 146 AQ2 PHE N 163 GLN N 173 1 11
HELIX 147 AQ3 SER N 195 LEU N 211 1 17
HELIX 148 AQ4 LEU N 267 GLY N 278 1 12
HELIX 149 AQ5 GLY N 278 ARG N 283 1 6
HELIX 150 AQ6 ARG N 284 THR N 293 5 10
HELIX 151 AQ7 ASP O 21 GLN O 39 1 19
HELIX 152 AQ8 TYR O 54 ALA O 58 5 5
HELIX 153 AQ9 ARG O 60 GLN O 65 1 6
HELIX 154 AR1 HIS O 73 GLY O 87 1 15
HELIX 155 AR2 GLU O 131 TYR O 135 5 5
HELIX 156 AR3 ILE O 157 TRP O 162 5 6
HELIX 157 AR4 PHE O 163 GLN O 173 1 11
HELIX 158 AR5 SER O 195 LEU O 211 1 17
HELIX 159 AR6 LEU O 267 GLY O 278 1 12
HELIX 160 AR7 GLY O 278 ARG O 283 1 6
HELIX 161 AR8 ARG O 284 THR O 293 5 10
HELIX 162 AR9 ASP P 21 GLN P 39 1 19
HELIX 163 AS1 ARG P 60 ALA P 67 5 8
HELIX 164 AS2 HIS P 73 GLY P 87 1 15
HELIX 165 AS3 GLU P 131 TYR P 135 5 5
HELIX 166 AS4 ILE P 157 TRP P 162 5 6
HELIX 167 AS5 PHE P 163 GLN P 173 1 11
HELIX 168 AS6 SER P 195 LEU P 211 1 17
HELIX 169 AS7 LEU P 267 GLY P 278 1 12
HELIX 170 AS8 GLY P 278 ARG P 283 1 6
HELIX 171 AS9 ARG P 284 THR P 293 5 10
SHEET 1 AA1 3 ILE A 43 LEU A 45 0
SHEET 2 AA1 3 LYS A 8 GLN A 15 1 N SER A 12 O LEU A 45
SHEET 3 AA1 3 ALA A 259 ASN A 266 -1 O PHE A 265 N VAL A 9
SHEET 1 AA2 4 LYS A 68 PRO A 69 0
SHEET 2 AA2 4 ILE A 90 ALA A 98 1 O GLU A 97 N LYS A 68
SHEET 3 AA2 4 ALA A 101 ILE A 109 -1 O ALA A 107 N VAL A 92
SHEET 4 AA2 4 ASP A 115 ARG A 120 -1 O LEU A 116 N ILE A 108
SHEET 1 AA3 6 VAL A 145 GLN A 147 0
SHEET 2 AA3 6 LYS A 152 VAL A 155 -1 O ILE A 153 N PHE A 146
SHEET 3 AA3 6 ILE A 177 THR A 182 1 O PHE A 179 N GLY A 154
SHEET 4 AA3 6 LEU A 214 ASN A 218 1 O SER A 217 N THR A 182
SHEET 5 AA3 6 PHE A 241 ALA A 243 -1 O ALA A 243 N LEU A 214
SHEET 6 AA3 6 ILE A 249 ILE A 252 -1 O VAL A 250 N ILE A 242
SHEET 1 AA4 3 GLY A 185 SER A 186 0
SHEET 2 AA4 3 SER A 232 TYR A 237 -1 O LYS A 235 N SER A 186
SHEET 3 AA4 3 ILE A 220 ILE A 225 -1 N GLY A 221 O PHE A 236
SHEET 1 AA5 3 ILE B 43 LEU B 45 0
SHEET 2 AA5 3 LYS B 8 GLN B 15 1 N SER B 12 O LEU B 45
SHEET 3 AA5 3 ALA B 259 ASN B 266 -1 O LEU B 261 N ALA B 13
SHEET 1 AA6 3 ILE B 90 ALA B 98 0
SHEET 2 AA6 3 ALA B 101 ILE B 109 -1 O ALA B 107 N VAL B 92
SHEET 3 AA6 3 ASP B 115 ARG B 120 -1 O LEU B 116 N ILE B 108
SHEET 1 AA7 6 VAL B 145 GLN B 147 0
SHEET 2 AA7 6 LYS B 152 VAL B 155 -1 O ILE B 153 N PHE B 146
SHEET 3 AA7 6 ILE B 177 THR B 182 1 O PHE B 179 N GLY B 154
SHEET 4 AA7 6 LEU B 214 ASN B 218 1 O VAL B 215 N LEU B 178
SHEET 5 AA7 6 PHE B 241 ALA B 243 -1 O ALA B 243 N LEU B 214
SHEET 6 AA7 6 ILE B 249 ILE B 252 -1 O VAL B 250 N ILE B 242
SHEET 1 AA8 2 ILE B 220 THR B 227 0
SHEET 2 AA8 2 GLY B 230 TYR B 237 -1 O PHE B 236 N GLY B 221
SHEET 1 AA9 3 ILE C 43 LEU C 45 0
SHEET 2 AA9 3 LYS C 8 GLN C 15 1 N SER C 12 O LEU C 45
SHEET 3 AA9 3 ALA C 259 ASN C 266 -1 O LEU C 261 N ALA C 13
SHEET 1 AB1 3 ILE C 90 ALA C 98 0
SHEET 2 AB1 3 ALA C 101 ILE C 109 -1 O ALA C 101 N ALA C 98
SHEET 3 AB1 3 ASP C 115 ARG C 120 -1 O LEU C 116 N ILE C 108
SHEET 1 AB2 6 VAL C 145 GLN C 147 0
SHEET 2 AB2 6 LYS C 152 VAL C 155 -1 O ILE C 153 N PHE C 146
SHEET 3 AB2 6 ILE C 177 PRO C 181 1 O ILE C 177 N GLY C 154
SHEET 4 AB2 6 LEU C 214 SER C 217 1 O VAL C 215 N LEU C 178
SHEET 5 AB2 6 PHE C 241 ALA C 243 -1 O ALA C 243 N LEU C 214
SHEET 6 AB2 6 ILE C 249 ILE C 252 -1 O VAL C 250 N ILE C 242
SHEET 1 AB3 2 ILE C 220 THR C 227 0
SHEET 2 AB3 2 GLY C 230 TYR C 237 -1 O PHE C 236 N GLY C 221
SHEET 1 AB4 3 ILE D 43 LEU D 45 0
SHEET 2 AB4 3 LYS D 8 GLN D 15 1 N SER D 12 O LEU D 45
SHEET 3 AB4 3 ALA D 259 ASN D 266 -1 O LEU D 261 N ALA D 13
SHEET 1 AB5 4 LYS D 68 PRO D 69 0
SHEET 2 AB5 4 ILE D 90 ALA D 98 1 O PHE D 95 N LYS D 68
SHEET 3 AB5 4 ALA D 101 ILE D 109 -1 O ALA D 107 N VAL D 92
SHEET 4 AB5 4 ASP D 115 ARG D 120 -1 O LEU D 116 N ILE D 108
SHEET 1 AB6 6 VAL D 145 GLN D 147 0
SHEET 2 AB6 6 LYS D 152 VAL D 155 -1 O ILE D 153 N PHE D 146
SHEET 3 AB6 6 ILE D 177 PRO D 181 1 O ILE D 177 N GLY D 154
SHEET 4 AB6 6 LEU D 214 SER D 217 1 O VAL D 215 N TYR D 180
SHEET 5 AB6 6 PHE D 241 ALA D 243 -1 O ALA D 243 N LEU D 214
SHEET 6 AB6 6 ILE D 249 ILE D 252 -1 O VAL D 250 N ILE D 242
SHEET 1 AB7 2 ILE D 220 THR D 227 0
SHEET 2 AB7 2 GLY D 230 TYR D 237 -1 O SER D 232 N ILE D 225
SHEET 1 AB8 3 ILE E 43 LEU E 45 0
SHEET 2 AB8 3 LYS E 8 GLN E 15 1 N SER E 12 O LEU E 45
SHEET 3 AB8 3 ALA E 259 ASN E 266 -1 O ALA E 263 N VAL E 11
SHEET 1 AB9 3 ILE E 90 ALA E 98 0
SHEET 2 AB9 3 ALA E 101 ILE E 109 -1 O ALA E 107 N VAL E 92
SHEET 3 AB9 3 ASP E 115 ARG E 120 -1 O LEU E 116 N ILE E 108
SHEET 1 AC1 6 VAL E 145 GLN E 147 0
SHEET 2 AC1 6 LYS E 152 VAL E 155 -1 O ILE E 153 N PHE E 146
SHEET 3 AC1 6 ILE E 177 THR E 182 1 O ILE E 177 N GLY E 154
SHEET 4 AC1 6 LEU E 214 ASN E 218 1 O SER E 217 N THR E 182
SHEET 5 AC1 6 PHE E 241 ALA E 243 -1 O PHE E 241 N ALA E 216
SHEET 6 AC1 6 ILE E 249 ILE E 252 -1 O SER E 251 N ILE E 242
SHEET 1 AC2 2 ILE E 220 THR E 227 0
SHEET 2 AC2 2 GLY E 230 TYR E 237 -1 O ILE E 234 N GLU E 223
SHEET 1 AC3 3 ILE F 43 LEU F 45 0
SHEET 2 AC3 3 LYS F 8 GLN F 15 1 N SER F 12 O LEU F 45
SHEET 3 AC3 3 ALA F 259 ASN F 266 -1 O ALA F 263 N VAL F 11
SHEET 1 AC4 3 ILE F 90 ALA F 98 0
SHEET 2 AC4 3 ALA F 101 ILE F 109 -1 O ALA F 107 N VAL F 92
SHEET 3 AC4 3 ASP F 115 ARG F 120 -1 O LEU F 116 N ILE F 108
SHEET 1 AC5 6 VAL F 145 GLN F 147 0
SHEET 2 AC5 6 LYS F 152 VAL F 155 -1 O ILE F 153 N PHE F 146
SHEET 3 AC5 6 ILE F 177 PRO F 181 1 O ILE F 177 N GLY F 154
SHEET 4 AC5 6 LEU F 214 SER F 217 1 O VAL F 215 N LEU F 178
SHEET 5 AC5 6 PHE F 241 ALA F 243 -1 O ALA F 243 N LEU F 214
SHEET 6 AC5 6 ILE F 249 ILE F 252 -1 O SER F 251 N ILE F 242
SHEET 1 AC6 2 ILE F 220 THR F 227 0
SHEET 2 AC6 2 GLY F 230 TYR F 237 -1 O PHE F 236 N GLY F 221
SHEET 1 AC7 3 ILE G 43 VAL G 44 0
SHEET 2 AC7 3 LYS G 8 SER G 12 1 N VAL G 10 O ILE G 43
SHEET 3 AC7 3 ALA G 263 ASN G 266 -1 O ALA G 263 N VAL G 11
SHEET 1 AC8 2 LEU G 14 GLN G 15 0
SHEET 2 AC8 2 ALA G 259 VAL G 260 -1 O ALA G 259 N GLN G 15
SHEET 1 AC9 4 LYS G 68 PRO G 69 0
SHEET 2 AC9 4 ILE G 90 ALA G 98 1 O GLU G 97 N LYS G 68
SHEET 3 AC9 4 ALA G 101 ILE G 109 -1 O TYR G 103 N GLU G 96
SHEET 4 AC9 4 ASP G 115 ARG G 120 -1 O TYR G 119 N ILE G 106
SHEET 1 AD1 6 VAL G 145 GLN G 147 0
SHEET 2 AD1 6 LYS G 152 VAL G 155 -1 O ILE G 153 N PHE G 146
SHEET 3 AD1 6 ILE G 177 THR G 182 1 O PHE G 179 N GLY G 154
SHEET 4 AD1 6 LEU G 214 ASN G 218 1 O VAL G 215 N TYR G 180
SHEET 5 AD1 6 PHE G 241 ALA G 243 -1 O ALA G 243 N LEU G 214
SHEET 6 AD1 6 ILE G 249 ILE G 252 -1 O SER G 251 N ILE G 242
SHEET 1 AD2 2 ASN G 222 THR G 227 0
SHEET 2 AD2 2 GLY G 230 LYS G 235 -1 O SER G 232 N ILE G 225
SHEET 1 AD3 3 ILE H 43 LEU H 45 0
SHEET 2 AD3 3 LYS H 8 GLN H 15 1 N SER H 12 O LEU H 45
SHEET 3 AD3 3 ALA H 259 VAL H 260 -1 O ALA H 259 N GLN H 15
SHEET 1 AD4 3 ILE H 43 LEU H 45 0
SHEET 2 AD4 3 LYS H 8 GLN H 15 1 N SER H 12 O LEU H 45
SHEET 3 AD4 3 ALA H 263 ASN H 266 -1 O ALA H 263 N VAL H 11
SHEET 1 AD5 3 ILE H 90 GLU H 97 0
SHEET 2 AD5 3 HIS H 102 ILE H 109 -1 O ALA H 107 N VAL H 92
SHEET 3 AD5 3 ASP H 115 ARG H 120 -1 O LEU H 116 N ILE H 108
SHEET 1 AD6 6 LYS H 144 GLN H 147 0
SHEET 2 AD6 6 LYS H 152 VAL H 155 -1 O ILE H 153 N PHE H 146
SHEET 3 AD6 6 ILE H 177 PHE H 179 1 O ILE H 177 N GLY H 154
SHEET 4 AD6 6 LEU H 214 ALA H 216 1 O VAL H 215 N LEU H 178
SHEET 5 AD6 6 PHE H 241 ALA H 243 -1 O PHE H 241 N ALA H 216
SHEET 6 AD6 6 ILE H 249 ILE H 252 -1 O VAL H 250 N ILE H 242
SHEET 1 AD7 2 ILE H 220 ASN H 222 0
SHEET 2 AD7 2 LYS H 235 TYR H 237 -1 O PHE H 236 N GLY H 221
SHEET 1 AD8 3 ILE I 43 LEU I 45 0
SHEET 2 AD8 3 LYS I 8 GLN I 15 1 N SER I 12 O LEU I 45
SHEET 3 AD8 3 ALA I 259 ASN I 266 -1 O LEU I 261 N ALA I 13
SHEET 1 AD9 3 ILE I 90 ALA I 98 0
SHEET 2 AD9 3 ALA I 101 ILE I 109 -1 O ALA I 107 N VAL I 92
SHEET 3 AD9 3 ASP I 115 ARG I 120 -1 O LEU I 116 N ILE I 108
SHEET 1 AE1 6 VAL I 145 GLN I 147 0
SHEET 2 AE1 6 LYS I 152 VAL I 155 -1 O ILE I 153 N PHE I 146
SHEET 3 AE1 6 ILE I 177 PRO I 181 1 O PHE I 179 N GLY I 154
SHEET 4 AE1 6 LEU I 214 SER I 217 1 O VAL I 215 N LEU I 178
SHEET 5 AE1 6 PHE I 241 ALA I 243 -1 O ALA I 243 N LEU I 214
SHEET 6 AE1 6 ILE I 249 ILE I 252 -1 O SER I 251 N ILE I 242
SHEET 1 AE2 3 GLY I 185 SER I 186 0
SHEET 2 AE2 3 SER I 232 TYR I 237 -1 O LYS I 235 N SER I 186
SHEET 3 AE2 3 ILE I 220 ILE I 225 -1 N ILE I 225 O SER I 232
SHEET 1 AE3 3 ILE J 43 LEU J 45 0
SHEET 2 AE3 3 LYS J 8 GLN J 15 1 N LEU J 14 O LEU J 45
SHEET 3 AE3 3 ALA J 259 ASN J 266 -1 O LEU J 261 N ALA J 13
SHEET 1 AE4 3 ILE J 90 ALA J 98 0
SHEET 2 AE4 3 ALA J 101 ILE J 109 -1 O ALA J 107 N VAL J 92
SHEET 3 AE4 3 ASP J 115 ARG J 120 -1 O LEU J 116 N ILE J 108
SHEET 1 AE5 6 VAL J 145 GLN J 147 0
SHEET 2 AE5 6 LYS J 152 VAL J 155 -1 O ILE J 153 N PHE J 146
SHEET 3 AE5 6 ILE J 177 THR J 182 1 O ILE J 177 N GLY J 154
SHEET 4 AE5 6 LEU J 214 ASN J 218 1 O SER J 217 N THR J 182
SHEET 5 AE5 6 PHE J 241 ALA J 243 -1 O ALA J 243 N LEU J 214
SHEET 6 AE5 6 ILE J 249 ILE J 252 -1 O VAL J 250 N ILE J 242
SHEET 1 AE6 2 ILE J 220 THR J 227 0
SHEET 2 AE6 2 GLY J 230 TYR J 237 -1 O GLY J 230 N THR J 227
SHEET 1 AE7 3 ILE K 43 LEU K 45 0
SHEET 2 AE7 3 LYS K 8 GLN K 15 1 N SER K 12 O LEU K 45
SHEET 3 AE7 3 ALA K 259 ASN K 266 -1 O LEU K 261 N ALA K 13
SHEET 1 AE8 3 ILE K 90 ALA K 98 0
SHEET 2 AE8 3 ALA K 101 ILE K 109 -1 O TYR K 103 N GLU K 96
SHEET 3 AE8 3 ASP K 115 ARG K 120 -1 O LEU K 116 N ILE K 108
SHEET 1 AE9 6 VAL K 145 GLN K 147 0
SHEET 2 AE9 6 LYS K 152 VAL K 155 -1 O ILE K 153 N PHE K 146
SHEET 3 AE9 6 LEU K 178 THR K 182 1 O PHE K 179 N GLY K 154
SHEET 4 AE9 6 LEU K 214 ASN K 218 1 O SER K 217 N THR K 182
SHEET 5 AE9 6 PHE K 241 ALA K 243 -1 O PHE K 241 N ALA K 216
SHEET 6 AE9 6 ILE K 249 ILE K 252 -1 O VAL K 250 N ILE K 242
SHEET 1 AF1 2 ILE K 220 THR K 227 0
SHEET 2 AF1 2 GLY K 230 TYR K 237 -1 O PHE K 236 N GLY K 221
SHEET 1 AF2 3 ILE L 43 LEU L 45 0
SHEET 2 AF2 3 LYS L 8 GLN L 15 1 N LEU L 14 O LEU L 45
SHEET 3 AF2 3 ALA L 259 ASN L 266 -1 O LEU L 261 N ALA L 13
SHEET 1 AF3 3 ILE L 90 ALA L 98 0
SHEET 2 AF3 3 ALA L 101 ILE L 109 -1 O ALA L 107 N VAL L 92
SHEET 3 AF3 3 ASP L 115 ARG L 120 -1 O LEU L 116 N ILE L 108
SHEET 1 AF4 6 VAL L 145 GLN L 147 0
SHEET 2 AF4 6 LYS L 152 VAL L 155 -1 O ILE L 153 N PHE L 146
SHEET 3 AF4 6 LEU L 178 THR L 182 1 O PHE L 179 N GLY L 154
SHEET 4 AF4 6 LEU L 214 ASN L 218 1 O VAL L 215 N TYR L 180
SHEET 5 AF4 6 PHE L 241 ALA L 243 -1 O ALA L 243 N LEU L 214
SHEET 6 AF4 6 ILE L 249 ILE L 252 -1 O VAL L 250 N ILE L 242
SHEET 1 AF5 2 ILE L 220 THR L 227 0
SHEET 2 AF5 2 GLY L 230 TYR L 237 -1 O PHE L 236 N GLY L 221
SHEET 1 AF6 3 ILE M 43 LEU M 45 0
SHEET 2 AF6 3 LYS M 8 GLN M 15 1 N LEU M 14 O LEU M 45
SHEET 3 AF6 3 ALA M 259 ASN M 266 -1 O LEU M 261 N ALA M 13
SHEET 1 AF7 4 LYS M 68 PRO M 69 0
SHEET 2 AF7 4 ILE M 90 ALA M 98 1 O PHE M 95 N LYS M 68
SHEET 3 AF7 4 ALA M 101 ILE M 109 -1 O ALA M 107 N VAL M 92
SHEET 4 AF7 4 ASP M 115 ARG M 120 -1 O LEU M 116 N ILE M 108
SHEET 1 AF8 6 VAL M 145 GLN M 147 0
SHEET 2 AF8 6 LYS M 152 VAL M 155 -1 O ILE M 153 N PHE M 146
SHEET 3 AF8 6 ILE M 177 THR M 182 1 O ILE M 177 N GLY M 154
SHEET 4 AF8 6 LEU M 214 ASN M 218 1 O VAL M 215 N TYR M 180
SHEET 5 AF8 6 PHE M 241 ALA M 243 -1 O PHE M 241 N ALA M 216
SHEET 6 AF8 6 ILE M 249 ILE M 252 -1 O VAL M 250 N ILE M 242
SHEET 1 AF9 2 ILE M 220 THR M 227 0
SHEET 2 AF9 2 GLY M 230 TYR M 237 -1 O SER M 232 N ILE M 225
SHEET 1 AG1 3 ILE N 43 LEU N 45 0
SHEET 2 AG1 3 LYS N 8 GLN N 15 1 N SER N 12 O LEU N 45
SHEET 3 AG1 3 ALA N 259 ASN N 266 -1 O ALA N 263 N VAL N 11
SHEET 1 AG2 3 ILE N 90 ALA N 98 0
SHEET 2 AG2 3 ALA N 101 ILE N 109 -1 O ALA N 107 N VAL N 92
SHEET 3 AG2 3 ASP N 115 ARG N 120 -1 O LEU N 116 N ILE N 108
SHEET 1 AG3 6 VAL N 145 GLN N 147 0
SHEET 2 AG3 6 LYS N 152 VAL N 155 -1 O ILE N 153 N PHE N 146
SHEET 3 AG3 6 ILE N 177 THR N 182 1 O ILE N 177 N GLY N 154
SHEET 4 AG3 6 LEU N 214 ASN N 218 1 O SER N 217 N THR N 182
SHEET 5 AG3 6 PHE N 241 ALA N 243 -1 O ALA N 243 N LEU N 214
SHEET 6 AG3 6 ILE N 249 ILE N 252 -1 O VAL N 250 N ILE N 242
SHEET 1 AG4 2 ILE N 220 THR N 227 0
SHEET 2 AG4 2 GLY N 230 TYR N 237 -1 O PHE N 236 N GLY N 221
SHEET 1 AG5 3 ILE O 43 LEU O 45 0
SHEET 2 AG5 3 LYS O 8 GLN O 15 1 O VAL O 10 N ILE O 43
SHEET 3 AG5 3 ALA O 259 ASN O 266 -1 O ALA O 263 N VAL O 11
SHEET 1 AG6 4 LYS O 68 PRO O 69 0
SHEET 2 AG6 4 ILE O 90 ALA O 98 1 O PHE O 95 N LYS O 68
SHEET 3 AG6 4 ALA O 101 ILE O 109 -1 O ALA O 107 N VAL O 92
SHEET 4 AG6 4 ASP O 115 ARG O 120 -1 O LEU O 116 N ILE O 108
SHEET 1 AG7 6 VAL O 145 GLN O 147 0
SHEET 2 AG7 6 LYS O 152 VAL O 155 -1 O ILE O 153 N PHE O 146
SHEET 3 AG7 6 ILE O 177 THR O 182 1 O ILE O 177 N GLY O 154
SHEET 4 AG7 6 LEU O 214 ASN O 218 1 O SER O 217 N THR O 182
SHEET 5 AG7 6 PHE O 241 ALA O 243 -1 O ALA O 243 N LEU O 214
SHEET 6 AG7 6 ILE O 249 ILE O 252 -1 O VAL O 250 N ILE O 242
SHEET 1 AG8 2 ILE O 220 THR O 227 0
SHEET 2 AG8 2 GLY O 230 TYR O 237 -1 O SER O 232 N ILE O 225
SHEET 1 AG9 3 ILE P 43 LEU P 45 0
SHEET 2 AG9 3 LYS P 8 GLN P 15 1 N SER P 12 O LEU P 45
SHEET 3 AG9 3 ALA P 259 VAL P 260 -1 O ALA P 259 N GLN P 15
SHEET 1 AH1 3 ILE P 43 LEU P 45 0
SHEET 2 AH1 3 LYS P 8 GLN P 15 1 N SER P 12 O LEU P 45
SHEET 3 AH1 3 ALA P 263 ASN P 266 -1 O ALA P 263 N VAL P 11
SHEET 1 AH2 3 ILE P 90 ALA P 98 0
SHEET 2 AH2 3 ALA P 101 ILE P 109 -1 O SER P 105 N PHE P 94
SHEET 3 AH2 3 ASP P 115 ARG P 120 -1 O LEU P 116 N ILE P 108
SHEET 1 AH3 6 VAL P 145 GLN P 147 0
SHEET 2 AH3 6 LYS P 152 VAL P 155 -1 O ILE P 153 N PHE P 146
SHEET 3 AH3 6 ILE P 177 PHE P 179 1 O PHE P 179 N GLY P 154
SHEET 4 AH3 6 LEU P 214 ALA P 216 1 O VAL P 215 N LEU P 178
SHEET 5 AH3 6 PHE P 241 ALA P 243 -1 O ALA P 243 N LEU P 214
SHEET 6 AH3 6 ILE P 249 ILE P 252 -1 O SER P 251 N ILE P 242
SHEET 1 AH4 2 ILE P 220 ILE P 225 0
SHEET 2 AH4 2 SER P 232 TYR P 237 -1 O ILE P 234 N GLU P 223
SITE 1 AC1 3 SER A 23 THR A 75 ARG A 78
SITE 1 AC2 5 TYR A 54 TYR A 130 ALA A 183 ILE A 184
SITE 2 AC2 5 GLY A 185
SITE 1 AC3 6 PRO A 285 ASP A 286 HOH A 538 PRO C 138
SITE 2 AC3 6 HOH D 583 HOH D 618
SITE 1 AC4 7 TRP A 277 ASP B 126 TYR B 130 GLU B 187
SITE 2 AC4 7 HOH B 505 HOH B 572 HOH B 604
SITE 1 AC5 6 MET A 273 TRP A 277 SER B 195 HIS B 198
SITE 2 AC5 6 HOH B 559 HOH B 561
SITE 1 AC6 3 ALA B 171 LEU B 172 ARG B 274
SITE 1 AC7 4 GLU B 51 ARG B 66 HOH B 551 HOH B 566
SITE 1 AC8 4 TYR B 70 HOH B 537 HOH B 571 HOH B 633
SITE 1 AC9 8 ASP C 126 TRP C 159 GLU C 187 HOH C 501
SITE 2 AC9 8 HOH C 544 HOH C 599 HOH C 643 TRP D 277
SITE 1 AD1 4 MET C 273 TRP C 277 HOH C 615 HIS D 198
SITE 1 AD2 4 SER C 23 THR C 75 ARG C 78 HOH C 527
SITE 1 AD3 4 TYR C 70 ASP C 115 LEU C 116 HOH C 683
SITE 1 AD4 6 PRO C 285 ASP C 286 HOH C 579 HOH C 616
SITE 2 AD4 6 HOH E 632 HOH F 531
SITE 1 AD5 6 TRP C 277 ASP D 126 TYR D 130 GLU D 187
SITE 2 AD5 6 HOH D 501 HOH D 648
SITE 1 AD6 6 ILE C 193 HIS C 198 MET D 273 TRP D 277
SITE 2 AD6 6 HOH D 542 HOH D 562
SITE 1 AD7 4 SER D 23 THR D 75 ARG D 78 HOH D 647
SITE 1 AD8 6 ARG C 201 HOH C 602 GLN D 204 GLU D 248
SITE 2 AD8 6 ILE D 249 HOH D 554
SITE 1 AD9 6 HOH A 521 VAL C 300 PRO D 285 ASP D 286
SITE 2 AD9 6 HOH D 543 HOH D 679
SITE 1 AE1 6 ASP E 126 TYR E 130 GLU E 187 HOH E 517
SITE 2 AE1 6 HOH E 542 TRP F 277
SITE 1 AE2 4 MET E 273 TRP E 277 HOH E 524 HIS F 198
SITE 1 AE3 5 SER E 23 PRO E 74 THR E 75 ARG E 78
SITE 2 AE3 5 HOH E 588
SITE 1 AE4 1 GLY E 113
SITE 1 AE5 9 TRP E 277 HOH E 649 ASP F 126 TYR F 130
SITE 2 AE5 9 TRP F 159 GLU F 187 HOH F 518 HOH F 581
SITE 3 AE5 9 HOH F 627
SITE 1 AE6 5 HIS E 198 MET F 273 TRP F 277 HOH F 503
SITE 2 AE6 5 HOH F 534
SITE 1 AE7 5 VAL F 22 SER F 23 PRO F 74 THR F 75
SITE 2 AE7 5 ARG F 78
SITE 1 AE8 7 PRO G 125 ASP G 126 TYR G 130 TRP G 159
SITE 2 AE8 7 GLU G 187 HOH G 540 TRP H 277
SITE 1 AE9 4 SER G 195 HIS G 198 MET H 273 TRP H 277
SITE 1 AF1 6 LYS G 256 GLU G 257 HOH G 519 HOH G 529
SITE 2 AF1 6 LEU L 32 GLU L 258
SITE 1 AF2 2 ARG G 7 GLN G 147
SITE 1 AF3 6 MET I 273 TRP I 277 HOH I 514 HOH I 540
SITE 2 AF3 6 HOH I 584 HIS J 198
SITE 1 AF4 4 SER I 23 PRO I 74 THR I 75 ARG I 78
SITE 1 AF5 5 PRO I 285 ASP I 286 HOH I 532 PRO K 138
SITE 2 AF5 5 HOH L 513
SITE 1 AF6 6 TRP I 277 HOH I 565 ASP J 126 GLU J 187
SITE 2 AF6 6 HOH J 527 HOH J 588
SITE 1 AF7 5 ALA J 171 ARG J 274 PHE J 280 HOH J 572
SITE 2 AF7 5 HOH J 606
SITE 1 AF8 1 ILE J 249
SITE 1 AF9 7 ASP K 126 TYR K 130 GLU K 187 HOH K 509
SITE 2 AF9 7 HOH K 597 HOH K 652 TRP L 277
SITE 1 AG1 6 MET K 273 TRP K 277 HOH K 525 HOH K 639
SITE 2 AG1 6 SER L 195 HIS L 198
SITE 1 AG2 5 SER K 23 THR K 75 ARG K 78 HOH K 502
SITE 2 AG2 5 HOH K 529
SITE 1 AG3 7 ARG K 283 PRO K 285 ASP K 286 HOH K 538
SITE 2 AG3 7 HOH K 584 HOH M 631 HOH N 513
SITE 1 AG4 9 TRP K 277 ASP L 126 TYR L 130 TRP L 159
SITE 2 AG4 9 GLU L 187 HOH L 507 HOH L 517 HOH L 603
SITE 3 AG4 9 HOH L 677
SITE 1 AG5 5 HIS K 198 MET L 273 TRP L 277 HOH L 557
SITE 2 AG5 5 HOH L 560
SITE 1 AG6 6 SER L 23 THR L 75 ARG L 78 HOH L 512
SITE 2 AG6 6 HOH L 543 HOH L 549
SITE 1 AG7 2 LYS L 81 ASP L 112
SITE 1 AG8 7 HOH J 616 VAL K 300 ARG L 283 PRO L 285
SITE 2 AG8 7 ASP L 286 HOH L 514 HOH L 579
SITE 1 AG9 7 ASP M 126 TYR M 130 TRP M 159 GLU M 187
SITE 2 AG9 7 HOH M 514 HOH M 595 TRP N 277
SITE 1 AH1 6 SER M 195 HIS M 198 HOH M 506 HOH M 596
SITE 2 AH1 6 MET N 273 TRP N 277
SITE 1 AH2 5 VAL M 22 SER M 23 THR M 75 ARG M 78
SITE 2 AH2 5 HOH M 524
SITE 1 AH3 8 TRP M 277 HOH M 579 ASP N 126 TYR N 130
SITE 2 AH3 8 TRP N 159 GLU N 187 HOH N 518 HOH N 559
SITE 1 AH4 4 TRP M 277 HIS N 198 HOH N 515 HOH N 557
SITE 1 AH5 6 SER N 23 PRO N 74 THR N 75 ARG N 78
SITE 2 AH5 6 HOH N 578 HOH N 609
SITE 1 AH6 1 HOH N 509
SITE 1 AH7 8 ASP O 126 TRP O 159 GLU O 187 HOH O 533
SITE 2 AH7 8 HOH O 580 HOH O 619 TRP P 277 HOH P 527
SITE 1 AH8 5 SER O 195 HIS O 198 MET P 273 TRP P 277
SITE 2 AH8 5 HOH P 509
CRYST1 152.531 210.756 208.723 90.00 90.00 90.00 P 21 21 2 64
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 0.006556 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
