HEADER CHAPERONE 20-DEC-12 3ZHA
TITLE MOLECULAR BASIS FOR THE ACTION OF THE COLLAGEN-SPECIFIC CHAPERONE
TITLE 2 HSP47 SERPINH1 AND ITS STRUCTURE-SPECIFIC CLIENT RECOGNITION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HSP47;
COMPND 3 CHAIN: A, B, C, D, K, L, P, Q;
COMPND 4 FRAGMENT: RESIDUES 36-418;
COMPND 5 SYNONYM: SERPIN PEPTIDASE INHIBITOR, CLADE H (HEAT SHOCK PROTEIN 47),
COMPND 6 MEMBER 1, COLLAGEN BINDING PROTEIN 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COLLAGEN MODEL PEPTIDE 18-T8R11;
COMPND 10 CHAIN: E, F, G, H, I, J, M, N, O, R, S, T;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630
KEYWDS COLLAGEN, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WIDMER,J.M.GEBAUER,U.BAUMANN
REVDAT 2 20-DEC-23 3ZHA 1 REMARK LINK
REVDAT 1 09-JAN-13 3ZHA 0
SPRSDE 09-JAN-13 3ZHA 4AWR
JRNL AUTH C.WIDMER,J.M.GEBAUER,E.BRUNSTEIN,S.ROSENBAUM,F.ZAUCKE,
JRNL AUTH 2 C.DROGEMULLER,T.LEEB,U.BAUMANN
JRNL TITL MOLECULAR BASIS FOR THE ACTION OF THE COLLAGEN-SPECIFIC
JRNL TITL 2 CHAPERONE HSP47/SERPINH1 AND ITS STRUCTURE-SPECIFIC CLIENT
JRNL TITL 3 RECOGNITION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 13243 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22847422
JRNL DOI 10.1073/PNAS.1208072109
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 113420
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.03
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7929
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2414
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7797
REMARK 3 BIN R VALUE (WORKING SET) : 0.2414
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24641
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10930
REMARK 3 B22 (A**2) : 6.25260
REMARK 3 B33 (A**2) : -6.14330
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.08610
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.387
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.567
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.251
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.672
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.261
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 25257 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 34132 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 8749 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 539 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 3651 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 25257 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 3172 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 27360 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.01
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 35
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 35-186
REMARK 3 ORIGIN FOR THE GROUP (A): -62.2493 -130.6810 -190.3748
REMARK 3 T TENSOR
REMARK 3 T11: 0.1583 T22: 0.1797
REMARK 3 T33: 0.1867 T12: -0.0926
REMARK 3 T13: -0.1709 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 4.0630 L22: 4.3880
REMARK 3 L33: 1.8355 L12: 0.5847
REMARK 3 L13: 0.6528 L23: -0.7957
REMARK 3 S TENSOR
REMARK 3 S11: -0.3529 S12: 0.4677 S13: -0.1398
REMARK 3 S21: -0.7715 S22: 0.3007 S23: 0.8730
REMARK 3 S31: 0.1598 S32: -0.2230 S33: 0.0521
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 187-416
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5900 -116.9420 -183.2844
REMARK 3 T TENSOR
REMARK 3 T11: 0.0865 T22: 0.0956
REMARK 3 T33: 0.0893 T12: 0.0010
REMARK 3 T13: -0.0954 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 2.2034 L22: 2.8399
REMARK 3 L33: 1.1893 L12: 0.4222
REMARK 3 L13: 0.5456 L23: 0.5216
REMARK 3 S TENSOR
REMARK 3 S11: -0.1479 S12: 0.0285 S13: 0.0788
REMARK 3 S21: -0.3560 S22: 0.0666 S23: 0.3972
REMARK 3 S31: -0.1743 S32: -0.0881 S33: 0.0814
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND RESID 35-204
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3084 -88.5114 -138.6249
REMARK 3 T TENSOR
REMARK 3 T11: 0.0831 T22: 0.3865
REMARK 3 T33: 0.1393 T12: -0.0358
REMARK 3 T13: -0.0098 T23: -0.0974
REMARK 3 L TENSOR
REMARK 3 L11: 4.9409 L22: 2.0993
REMARK 3 L33: 4.0812 L12: 0.6128
REMARK 3 L13: 0.1928 L23: 0.7803
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: -0.7726 S13: 0.1426
REMARK 3 S21: 0.2038 S22: 0.0469 S23: -0.2532
REMARK 3 S31: -0.0941 S32: 0.7152 S33: -0.0899
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 205-365
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7180 -95.7892 -149.6945
REMARK 3 T TENSOR
REMARK 3 T11: 0.0464 T22: 0.2000
REMARK 3 T33: 0.1118 T12: 0.0035
REMARK 3 T13: -0.0220 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.6665 L22: 1.3631
REMARK 3 L33: 1.9254 L12: 0.3452
REMARK 3 L13: -0.2688 L23: 0.9723
REMARK 3 S TENSOR
REMARK 3 S11: 0.0851 S12: -0.2739 S13: 0.0688
REMARK 3 S21: 0.2312 S22: 0.0077 S23: -0.0411
REMARK 3 S31: 0.0813 S32: 0.1669 S33: -0.0928
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN C AND RESID 36-195
REMARK 3 ORIGIN FOR THE GROUP (A): -82.4950 -119.6880 -106.7578
REMARK 3 T TENSOR
REMARK 3 T11: 0.2999 T22: 0.2582
REMARK 3 T33: 0.7501 T12: 0.0539
REMARK 3 T13: -0.3185 T23: -0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 2.1477 L22: 4.4036
REMARK 3 L33: 1.2860 L12: -0.5587
REMARK 3 L13: 0.2326 L23: -0.1652
REMARK 3 S TENSOR
REMARK 3 S11: 0.1469 S12: 0.1470 S13: -0.3262
REMARK 3 S21: -0.7688 S22: -0.1366 S23: 1.3741
REMARK 3 S31: 0.0440 S32: -0.3791 S33: -0.0103
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN C AND RESID 196-366
REMARK 3 ORIGIN FOR THE GROUP (A): -70.9271 -106.0520 -101.1136
REMARK 3 T TENSOR
REMARK 3 L TENSOR
REMARK 3 S TENSOR
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND RESID 367-414
REMARK 3 ORIGIN FOR THE GROUP (A): -63.3599 -102.3350 -100.0770
REMARK 3 T TENSOR
REMARK 3 T11: 0.2012 T22: 0.1710
REMARK 3 T33: 0.2657 T12: 0.0327
REMARK 3 T13: -0.1253 T23: -0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 1.9254 L22: 3.4203
REMARK 3 L33: 0.4236 L12: -0.6382
REMARK 3 L13: -0.0658 L23: 0.0936
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.1439 S13: -0.1498
REMARK 3 S21: -0.4826 S22: -0.0252 S23: 0.6367
REMARK 3 S31: -0.1340 S32: -0.1574 S33: 0.0455
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN D AND RESID 35-120
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0897 -83.7474 -50.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1859 T22: 0.1252
REMARK 3 T33: 0.1894 T12: 0.0737
REMARK 3 T13: -0.0847 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 2.5886 L22: 4.4849
REMARK 3 L33: 1.9585 L12: 0.4821
REMARK 3 L13: 0.2473 L23: 0.9558
REMARK 3 S TENSOR
REMARK 3 S11: 0.1399 S12: 0.1365 S13: 0.0603
REMARK 3 S21: -0.5502 S22: -0.1332 S23: -0.1325
REMARK 3 S31: -0.0898 S32: 0.0606 S33: -0.0068
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN D AND RESID 126-203
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9785 -71.4065 -60.2727
REMARK 3 T TENSOR
REMARK 3 T11: 0.3074 T22: 0.5364
REMARK 3 T33: 0.1963 T12: -0.0332
REMARK 3 T13: -0.0106 T23: 0.0642
REMARK 3 L TENSOR
REMARK 3 L11: 2.6163 L22: 0.8154
REMARK 3 L33: 3.0667 L12: 0.6198
REMARK 3 L13: -1.0065 L23: 0.1733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0853 S12: -0.7630 S13: -0.4615
REMARK 3 S21: 0.3335 S22: -0.1075 S23: 0.0306
REMARK 3 S31: 0.0964 S32: 0.6492 S33: 0.0223
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN D AND RESID 204-364
REMARK 3 ORIGIN FOR THE GROUP (A): -42.9291 -84.6834 -66.5053
REMARK 3 T TENSOR
REMARK 3 T11: 0.2154 T22: 0.4571
REMARK 3 T33: 0.1983 T12: -0.1930
REMARK 3 T13: -0.0237 T23: -0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 4.4903 L22: 2.4840
REMARK 3 L33: 5.1431 L12: 0.5838
REMARK 3 L13: 0.0404 L23: -1.7472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: -0.2501 S13: 0.8256
REMARK 3 S21: 0.2233 S22: 0.1255 S23: -0.2992
REMARK 3 S31: -0.7150 S32: 0.8821 S33: -0.1293
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN D AND RESID 365-412
REMARK 3 ORIGIN FOR THE GROUP (A): -45.1472 -89.6458 -72.3473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1846 T22: 0.2289
REMARK 3 T33: 0.1679 T12: 0.0040
REMARK 3 T13: 0.0019 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.4151 L22: 1.2941
REMARK 3 L33: 2.6302 L12: 0.3676
REMARK 3 L13: 0.0412 L23: 1.2434
REMARK 3 S TENSOR
REMARK 3 S11: 0.0658 S12: -0.2984 S13: -0.0161
REMARK 3 S21: 0.2870 S22: 0.0088 S23: -0.0281
REMARK 3 S31: 0.0010 S32: 0.1999 S33: -0.0745
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN E AND RESID 0-17
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4376 -105.9180 -172.4381
REMARK 3 T TENSOR
REMARK 3 T11: 0.1628 T22: 0.2509
REMARK 3 T33: 0.2088 T12: 0.0090
REMARK 3 T13: 0.0334 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 4.9507 L22: 0.4059
REMARK 3 L33: 2.3319 L12: 1.3145
REMARK 3 L13: 2.2371 L23: 1.9100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: -0.0280 S13: -0.3479
REMARK 3 S21: -0.0236 S22: 0.1314 S23: -0.2717
REMARK 3 S31: 0.2023 S32: 0.3579 S33: -0.1901
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN F AND RESID 0-16
REMARK 3 ORIGIN FOR THE GROUP (A): -32.5374 -103.6280 -172.8526
REMARK 3 T TENSOR
REMARK 3 T11: 0.1604 T22: 0.1890
REMARK 3 T33: 0.2451 T12: -0.0867
REMARK 3 T13: 0.0039 T23: -0.0663
REMARK 3 L TENSOR
REMARK 3 L11: -0.7105 L22: 1.7575
REMARK 3 L33: 3.3299 L12: 2.0440
REMARK 3 L13: 1.9926 L23: 0.7128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: -0.1382 S13: 0.2705
REMARK 3 S21: -0.4766 S22: 0.1517 S23: -0.2438
REMARK 3 S31: -0.2863 S32: 0.0292 S33: -0.0696
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN G AND RESID 0-15
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4012 -103.0090 -170.1585
REMARK 3 T TENSOR
REMARK 3 T11: 0.1381 T22: 0.2425
REMARK 3 T33: 0.0824 T12: -0.0765
REMARK 3 T13: -0.0811 T23: 0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 2.2422 L22: 3.8221
REMARK 3 L33: 1.4099 L12: 3.4390
REMARK 3 L13: 3.1070 L23: -0.6313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.3615 S13: -0.2873
REMARK 3 S21: -0.2075 S22: -0.0372 S23: 0.3296
REMARK 3 S31: -0.2799 S32: -0.0872 S33: 0.0411
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN H AND RESID 0-17
REMARK 3 ORIGIN FOR THE GROUP (A): -52.7494 -94.7752 -89.2739
REMARK 3 T TENSOR
REMARK 3 T11: 0.1123 T22: 0.2305
REMARK 3 T33: 0.1547 T12: -0.0230
REMARK 3 T13: -0.0088 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.2598 L22: 1.2861
REMARK 3 L33: 2.6349 L12: 2.7901
REMARK 3 L13: 0.6707 L23: 0.9295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: -0.0376 S13: -0.1997
REMARK 3 S21: 0.0962 S22: -0.0890 S23: 0.2692
REMARK 3 S31: -0.2511 S32: -0.0918 S33: 0.0404
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN I AND RESID 1-16
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8905 -92.4957 -89.7846
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.2067
REMARK 3 T33: 0.2356 T12: -0.0535
REMARK 3 T13: -0.0077 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 1.8889 L22: 0.8047
REMARK 3 L33: 2.0948 L12: 2.7078
REMARK 3 L13: 1.5945 L23: -1.9390
REMARK 3 S TENSOR
REMARK 3 S11: 0.1926 S12: -0.0270 S13: 0.2580
REMARK 3 S21: -0.1667 S22: 0.0209 S23: -0.1056
REMARK 3 S31: -0.1457 S32: -0.0341 S33: -0.2135
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN J AND RESID 0-15
REMARK 3 ORIGIN FOR THE GROUP (A): -52.7448 -91.8842 -87.0401
REMARK 3 T TENSOR
REMARK 3 T11: 0.0705 T22: 0.0935
REMARK 3 T33: 0.1040 T12: -0.0537
REMARK 3 T13: -0.0768 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 1.8194 L22: 4.4217
REMARK 3 L33: 0.8749 L12: 0.8399
REMARK 3 L13: 2.0151 L23: -0.9282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.0475 S13: -0.1483
REMARK 3 S21: -0.0312 S22: 0.0599 S23: 0.0189
REMARK 3 S31: -0.3352 S32: 0.0282 S33: -0.0228
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN K AND RESID 35-207
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0818 -28.9100 -192.4508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1350 T22: 0.1736
REMARK 3 T33: 0.2203 T12: 0.0338
REMARK 3 T13: 0.0076 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.2012 L22: 1.7443
REMARK 3 L33: 2.5575 L12: 3.9970
REMARK 3 L13: 0.7832 L23: 1.3000
REMARK 3 S TENSOR
REMARK 3 S11: 0.1662 S12: -0.2493 S13: -0.1948
REMARK 3 S21: -0.1622 S22: -0.0792 S23: 0.2731
REMARK 3 S31: -0.1821 S32: -0.0160 S33: -0.0870
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN K AND RESID 208-366
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4708 -44.4088 -188.0899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0957 T22: 0.2146
REMARK 3 T33: 0.1379 T12: -0.0691
REMARK 3 T13: 0.1133 T23: -0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 4.1250 L22: 2.9753
REMARK 3 L33: 1.7501 L12: 0.2354
REMARK 3 L13: -0.5428 L23: 1.5470
REMARK 3 S TENSOR
REMARK 3 S11: -0.1239 S12: 0.2176 S13: 0.2872
REMARK 3 S21: -0.4397 S22: 0.3536 S23: -0.4947
REMARK 3 S31: -0.2747 S32: 0.3630 S33: -0.2297
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN K AND RESID 367-414
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2838 -47.3335 -186.6671
REMARK 3 T TENSOR
REMARK 3 T11: 0.0654 T22: 0.1630
REMARK 3 T33: 0.0114 T12: 0.0201
REMARK 3 T13: 0.0466 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.7233 L22: 1.7061
REMARK 3 L33: 0.9996 L12: 0.4780
REMARK 3 L13: -0.5091 L23: 0.5048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0556 S13: -0.0515
REMARK 3 S21: -0.1158 S22: 0.0723 S23: -0.2931
REMARK 3 S31: 0.0969 S32: 0.2901 S33: -0.0741
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN L AND RESID 35-166
REMARK 3 ORIGIN FOR THE GROUP (A): -58.8715 -72.6492 -136.7256
REMARK 3 T TENSOR
REMARK 3 T11: 0.0201 T22: 0.0436
REMARK 3 T33: -0.0550 T12: -0.0064
REMARK 3 T13: 0.0825 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 5.9342 L22: 2.8188
REMARK 3 L33: 3.1892 L12: 1.3358
REMARK 3 L13: 0.8461 L23: -0.1382
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: -0.0561 S13: 0.0980
REMARK 3 S21: -0.1093 S22: 0.1149 S23: 0.1085
REMARK 3 S31: 0.0928 S32: 0.0443 S33: -0.0440
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN L AND RESID 167-276
REMARK 3 ORIGIN FOR THE GROUP (A): -50.5441 -68.5052 -156.7351
REMARK 3 T TENSOR
REMARK 3 T11: 0.1831 T22: 0.6177
REMARK 3 T33: -0.0209 T12: -0.1391
REMARK 3 T13: 0.0654 T23: 0.0934
REMARK 3 L TENSOR
REMARK 3 L11: 4.1824 L22: 3.2751
REMARK 3 L33: 2.3649 L12: 0.7178
REMARK 3 L13: 1.1555 L23: -0.2007
REMARK 3 S TENSOR
REMARK 3 S11: 0.4231 S12: -1.3346 S13: -0.1811
REMARK 3 S21: 0.7300 S22: -0.2261 S23: 0.4085
REMARK 3 S31: 0.1943 S32: -0.7898 S33: -0.1970
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN L AND RESID 277-414
REMARK 3 ORIGIN FOR THE GROUP (A): -48.3556 -69.9823 -148.1158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.1620
REMARK 3 T33: 0.1085 T12: -0.0195
REMARK 3 T13: -0.0200 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.4417 L22: 0.9940
REMARK 3 L33: 2.0995 L12: -0.2661
REMARK 3 L13: 0.3274 L23: -0.9186
REMARK 3 S TENSOR
REMARK 3 S11: 0.1699 S12: -0.1333 S13: -0.1066
REMARK 3 S21: -0.0708 S22: -0.0574 S23: -0.0229
REMARK 3 S31: 0.2435 S32: 0.0509 S33: -0.1125
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN M AND RESID 1-17
REMARK 3 ORIGIN FOR THE GROUP (A): -41.4046 -56.0352 -175.3843
REMARK 3 T TENSOR
REMARK 3 T11: 0.0921 T22: 0.2433
REMARK 3 T33: -0.0073 T12: -0.0280
REMARK 3 T13: -0.0243 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 3.7691 L22: 1.6514
REMARK 3 L33: 2.5280 L12: 0.5311
REMARK 3 L13: 0.7512 L23: -0.8336
REMARK 3 S TENSOR
REMARK 3 S11: 0.2655 S12: -0.7969 S13: -0.2238
REMARK 3 S21: 0.3172 S22: -0.1576 S23: -0.1034
REMARK 3 S31: 0.1080 S32: -0.1441 S33: -0.1079
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN N AND RESID 1-17
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1008 -59.2391 -175.6210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.1274
REMARK 3 T33: 0.0256 T12: -0.0108
REMARK 3 T13: 0.0742 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: -0.2264 L22: 1.8256
REMARK 3 L33: 4.0656 L12: 1.9247
REMARK 3 L13: -0.0320 L23: -0.4101
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: -0.1562 S13: 0.0867
REMARK 3 S21: -0.1078 S22: 0.0122 S23: 0.1873
REMARK 3 S31: 0.2348 S32: 0.3443 S33: -0.0336
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN O AND RESID 1-17
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7837 -61.1214 -173.3090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1102 T22: 0.1777
REMARK 3 T33: 0.1210 T12: 0.0682
REMARK 3 T13: 0.0305 T23: -0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 2.4658 L22: 2.1140
REMARK 3 L33: 1.2735 L12: -1.9115
REMARK 3 L13: -5.2090 L23: 1.5275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: -0.0415 S13: 0.0040
REMARK 3 S21: -0.0118 S22: -0.1016 S23: -0.2814
REMARK 3 S31: 0.5396 S32: 0.2679 S33: 0.1511
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN P AND RESID 37-158
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0047 -19.2057 -114.1034
REMARK 3 T TENSOR
REMARK 3 T11: 0.0696 T22: 0.2188
REMARK 3 T33: 0.0905 T12: 0.0793
REMARK 3 T13: 0.1219 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: -1.6549 L22: 1.1563
REMARK 3 L33: 3.8035 L12: 3.2177
REMARK 3 L13: 3.9549 L23: -3.4989
REMARK 3 S TENSOR
REMARK 3 S11: -0.0453 S12: 0.1301 S13: -0.5590
REMARK 3 S21: 0.2309 S22: -0.0114 S23: -0.2999
REMARK 3 S31: 0.3382 S32: 0.4229 S33: 0.0567
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN P AND RESID 159-339
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3750 -30.0092 -102.6862
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.3994
REMARK 3 T33: 0.4255 T12: 0.0115
REMARK 3 T13: 0.2029 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 6.1821 L22: 5.2185
REMARK 3 L33: 2.8875 L12: 1.5520
REMARK 3 L13: -2.3263 L23: 0.4011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 1.0259 S13: 0.1823
REMARK 3 S21: -0.9161 S22: 0.2428 S23: -1.1054
REMARK 3 S31: -0.2028 S32: 0.0264 S33: -0.2446
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN P AND RESID 340- 414
REMARK 3 ORIGIN FOR THE GROUP (A): -47.7036 -30.1518 -103.8248
REMARK 3 T TENSOR
REMARK 3 T11: 0.1695 T22: 0.1788
REMARK 3 T33: 0.3203 T12: 0.0863
REMARK 3 T13: 0.0396 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 2.9697 L22: 2.6107
REMARK 3 L33: 1.0732 L12: 1.1096
REMARK 3 L13: 0.0837 L23: 0.2807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0765 S12: -0.0447 S13: -0.2194
REMARK 3 S21: -0.1586 S22: 0.1228 S23: -0.5572
REMARK 3 S31: 0.1972 S32: 0.2490 S33: -0.0463
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN Q AND RESID 35-165
REMARK 3 ORIGIN FOR THE GROUP (A): -78.3255 -61.7730 -53.0769
REMARK 3 T TENSOR
REMARK 3 T11: 0.2257 T22: 0.2146
REMARK 3 T33: 0.2175 T12: 0.0497
REMARK 3 T13: 0.0327 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 5.3110 L22: 3.6197
REMARK 3 L33: 1.1649 L12: 1.5837
REMARK 3 L13: -0.7547 L23: -0.1121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0572 S12: 0.1024 S13: 0.1471
REMARK 3 S21: -0.1806 S22: 0.1042 S23: -0.3073
REMARK 3 S31: 0.1312 S32: 0.0731 S33: -0.1614
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN Q AND RESID 166-311
REMARK 3 ORIGIN FOR THE GROUP (A): -68.3358 -55.7415 -72.4899
REMARK 3 T TENSOR
REMARK 3 T11: 0.1749 T22: 0.4022
REMARK 3 T33: 0.0704 T12: -0.0341
REMARK 3 T13: 0.0839 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 3.7684 L22: 2.6812
REMARK 3 L33: 2.7203 L12: 0.0030
REMARK 3 L13: 1.3315 L23: 0.5897
REMARK 3 S TENSOR
REMARK 3 S11: 0.1398 S12: -1.0953 S13: -0.1288
REMARK 3 S21: 0.2397 S22: -0.0567 S23: 0.2821
REMARK 3 S31: 0.2024 S32: -0.5402 S33: -0.0832
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN Q AND RESID 312-411
REMARK 3 ORIGIN FOR THE GROUP (A): -71.5505 -62.3723 -63.7335
REMARK 3 T TENSOR
REMARK 3 T11: 0.2179 T22: 0.1479
REMARK 3 T33: 0.2315 T12: 0.0195
REMARK 3 T13: -0.0125 T23: -0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 2.1310 L22: 1.5387
REMARK 3 L33: 1.9653 L12: -0.2740
REMARK 3 L13: 0.3931 L23: -1.2116
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: -0.2028 S13: 0.1288
REMARK 3 S21: 0.1019 S22: -0.0814 S23: -0.0557
REMARK 3 S31: 0.0873 S32: 0.1006 S33: 0.0497
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN R AND RESID 0-16
REMARK 3 ORIGIN FOR THE GROUP (A): -61.5558 -44.9316 -92.4497
REMARK 3 T TENSOR
REMARK 3 T11: 0.2613 T22: 0.2094
REMARK 3 T33: 0.2220 T12: 0.0076
REMARK 3 T13: 0.0244 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 2.4982 L22: 1.0545
REMARK 3 L33: 2.5163 L12: 0.5759
REMARK 3 L13: 0.3029 L23: -1.0331
REMARK 3 S TENSOR
REMARK 3 S11: 0.1359 S12: -0.4901 S13: -0.3035
REMARK 3 S21: 0.2632 S22: -0.0311 S23: 0.0331
REMARK 3 S31: 0.1449 S32: -0.2292 S33: -0.1048
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN S AND RESID 0-16
REMARK 3 ORIGIN FOR THE GROUP (A): -61.5800 -47.3535 -93.1854
REMARK 3 T TENSOR
REMARK 3 T11: 0.0837 T22: 0.2104
REMARK 3 T33: 0.1965 T12: -0.0894
REMARK 3 T13: 0.0165 T23: 0.1118
REMARK 3 L TENSOR
REMARK 3 L11: -0.0830 L22: 3.3670
REMARK 3 L33: 5.1410 L12: 1.5681
REMARK 3 L13: -0.4569 L23: 0.7149
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: 0.0367 S13: 0.1682
REMARK 3 S21: -0.2535 S22: 0.0190 S23: 0.0463
REMARK 3 S31: 0.0697 S32: 0.1712 S33: -0.0836
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN T AND RESID 0-16
REMARK 3 ORIGIN FOR THE GROUP (A): -60.1827 -49.0528 -90.3957
REMARK 3 T TENSOR
REMARK 3 T11: 0.1660 T22: 0.2851
REMARK 3 T33: 0.1539 T12: 0.0147
REMARK 3 T13: 0.0148 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 1.9884 L22: 0.5408
REMARK 3 L33: 0.5423 L12: 2.1314
REMARK 3 L13: -2.9481 L23: 0.2706
REMARK 3 S TENSOR
REMARK 3 S11: -0.0854 S12: -0.1419 S13: 0.1068
REMARK 3 S21: -0.0105 S22: -0.0787 S23: 0.1075
REMARK 3 S31: 0.1058 S32: 0.1651 S33: 0.1641
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 3ZHA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1290055214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113422
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 1.08000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4AU2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R, S, T
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, I, J
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O
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 ASN A 120
REMARK 465 SER A 121
REMARK 465 THR A 122
REMARK 465 ALA A 123
REMARK 465 ARG A 124
REMARK 465 ASN A 125
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 ASN B 120
REMARK 465 SER B 121
REMARK 465 THR B 122
REMARK 465 ALA B 123
REMARK 465 ASP B 367
REMARK 465 GLN B 368
REMARK 465 ASP B 369
REMARK 465 ILE B 370
REMARK 465 TYR B 371
REMARK 465 GLY B 372
REMARK 465 ARG B 373
REMARK 465 GLU B 374
REMARK 465 GLU B 375
REMARK 465 LEU B 376
REMARK 465 LYS B 413
REMARK 465 MET B 414
REMARK 465 ARG B 415
REMARK 465 ASP B 416
REMARK 465 GLU B 417
REMARK 465 LEU B 418
REMARK 465 LEU B 419
REMARK 465 GLU B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 HIS B 426
REMARK 465 MET C 35
REMARK 465 ASN C 120
REMARK 465 SER C 121
REMARK 465 THR C 122
REMARK 465 ALA C 123
REMARK 465 ARG C 124
REMARK 465 ASN C 125
REMARK 465 LEU C 418
REMARK 465 LEU C 419
REMARK 465 GLU C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 HIS C 423
REMARK 465 HIS C 424
REMARK 465 HIS C 425
REMARK 465 HIS C 426
REMARK 465 SER D 121
REMARK 465 THR D 122
REMARK 465 ASP D 369
REMARK 465 ILE D 370
REMARK 465 TYR D 371
REMARK 465 GLY D 372
REMARK 465 ARG D 373
REMARK 465 GLU D 374
REMARK 465 GLU D 375
REMARK 465 LEU D 376
REMARK 465 LYS D 413
REMARK 465 MET D 414
REMARK 465 ARG D 415
REMARK 465 ASP D 416
REMARK 465 GLU D 417
REMARK 465 LEU D 418
REMARK 465 LEU D 419
REMARK 465 GLU D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
REMARK 465 HIS D 423
REMARK 465 HIS D 424
REMARK 465 HIS D 425
REMARK 465 HIS D 426
REMARK 465 NH2 E 18
REMARK 465 PRO F 17
REMARK 465 NH2 F 18
REMARK 465 PRO G 16
REMARK 465 PRO G 17
REMARK 465 NH2 G 18
REMARK 465 NH2 H 18
REMARK 465 PRO I 17
REMARK 465 NH2 I 18
REMARK 465 PRO J 16
REMARK 465 PRO J 17
REMARK 465 NH2 J 18
REMARK 465 SER K 121
REMARK 465 THR K 122
REMARK 465 ALA K 123
REMARK 465 ARG K 124
REMARK 465 ASN K 125
REMARK 465 VAL K 126
REMARK 465 ARG K 415
REMARK 465 ASP K 416
REMARK 465 GLU K 417
REMARK 465 LEU K 418
REMARK 465 LEU K 419
REMARK 465 GLU K 420
REMARK 465 HIS K 421
REMARK 465 HIS K 422
REMARK 465 HIS K 423
REMARK 465 HIS K 424
REMARK 465 HIS K 425
REMARK 465 HIS K 426
REMARK 465 SER L 121
REMARK 465 THR L 122
REMARK 465 ALA L 123
REMARK 465 TYR L 371
REMARK 465 GLY L 372
REMARK 465 ARG L 373
REMARK 465 GLU L 374
REMARK 465 GLU L 375
REMARK 465 LEU L 376
REMARK 465 ARG L 377
REMARK 465 SER L 378
REMARK 465 ARG L 415
REMARK 465 ASP L 416
REMARK 465 GLU L 417
REMARK 465 LEU L 418
REMARK 465 LEU L 419
REMARK 465 GLU L 420
REMARK 465 HIS L 421
REMARK 465 HIS L 422
REMARK 465 HIS L 423
REMARK 465 HIS L 424
REMARK 465 HIS L 425
REMARK 465 HIS L 426
REMARK 465 NH2 M 18
REMARK 465 NH2 N 18
REMARK 465 NH2 O 18
REMARK 465 MET P 35
REMARK 465 LEU P 36
REMARK 465 SER P 121
REMARK 465 THR P 122
REMARK 465 ALA P 123
REMARK 465 ARG P 124
REMARK 465 ASN P 125
REMARK 465 VAL P 126
REMARK 465 ASP P 416
REMARK 465 GLU P 417
REMARK 465 LEU P 418
REMARK 465 LEU P 419
REMARK 465 GLU P 420
REMARK 465 HIS P 421
REMARK 465 HIS P 422
REMARK 465 HIS P 423
REMARK 465 HIS P 424
REMARK 465 HIS P 425
REMARK 465 HIS P 426
REMARK 465 SER Q 121
REMARK 465 THR Q 122
REMARK 465 ALA Q 123
REMARK 465 ARG Q 124
REMARK 465 ILE Q 370
REMARK 465 TYR Q 371
REMARK 465 GLY Q 372
REMARK 465 ARG Q 373
REMARK 465 GLU Q 374
REMARK 465 GLU Q 375
REMARK 465 LEU Q 376
REMARK 465 ARG Q 377
REMARK 465 ASP Q 412
REMARK 465 LYS Q 413
REMARK 465 MET Q 414
REMARK 465 ARG Q 415
REMARK 465 ASP Q 416
REMARK 465 GLU Q 417
REMARK 465 LEU Q 418
REMARK 465 LEU Q 419
REMARK 465 GLU Q 420
REMARK 465 HIS Q 421
REMARK 465 HIS Q 422
REMARK 465 HIS Q 423
REMARK 465 HIS Q 424
REMARK 465 HIS Q 425
REMARK 465 HIS Q 426
REMARK 465 NH2 R 18
REMARK 465 NH2 S 18
REMARK 465 PRO T 17
REMARK 465 NH2 T 18
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 377 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 415 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 416 CG OD1 OD2
REMARK 470 GLU A 417 CG CD OE1 OE2
REMARK 470 LEU A 419 CG CD1 CD2
REMARK 470 GLU A 420 CG CD OE1 OE2
REMARK 470 ARG B 124 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 125 CG OD1 ND2
REMARK 470 ARG B 377 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 415 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 416 CG OD1 OD2
REMARK 470 GLU C 417 CG CD OE1 OE2
REMARK 470 ARG D 377 CG CD NE CZ NH1 NH2
REMARK 470 MET L 35 CG SD CE
REMARK 470 ARG L 124 CG CD NE CZ NH1 NH2
REMARK 470 ARG P 377 CG CD NE CZ NH1 NH2
REMARK 470 ARG P 415 CG CD NE CZ NH1 NH2
REMARK 470 SER Q 378 OG
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 GLU A 65 -88.59 -100.50
REMARK 500 ALA A 87 -121.11 46.57
REMARK 500 ALA A 99 36.75 -99.99
REMARK 500 VAL A 188 -71.23 -92.56
REMARK 500 ALA A 261 123.92 -39.72
REMARK 500 LEU A 285 95.53 -68.35
REMARK 500 SER A 341 -54.40 -140.46
REMARK 500 GLU A 374 0.36 -55.17
REMARK 500 GLU B 65 -90.74 -100.78
REMARK 500 ALA B 87 -122.29 48.04
REMARK 500 LEU B 118 59.16 -93.98
REMARK 500 VAL B 188 -71.10 -92.65
REMARK 500 LEU B 285 95.10 -68.46
REMARK 500 SER B 341 -53.44 -140.43
REMARK 500 GLN B 396 -70.07 -73.86
REMARK 500 GLU C 65 -90.02 -100.59
REMARK 500 ALA C 87 -127.41 55.96
REMARK 500 VAL C 188 -72.12 -93.45
REMARK 500 LEU C 285 95.09 -67.63
REMARK 500 SER C 341 -55.12 -136.80
REMARK 500 ASP C 367 109.18 -59.32
REMARK 500 GLN C 368 -7.88 -58.01
REMARK 500 ARG C 373 48.21 -89.29
REMARK 500 GLU D 65 -89.14 -99.28
REMARK 500 ALA D 87 -125.73 48.56
REMARK 500 ALA D 99 41.73 -98.85
REMARK 500 ARG D 124 -71.60 -54.67
REMARK 500 VAL D 188 -72.23 -93.24
REMARK 500 ALA D 261 123.84 -38.39
REMARK 500 LEU D 285 95.57 -69.25
REMARK 500 SER D 341 -54.40 -139.02
REMARK 500 GLU K 65 -90.60 -100.44
REMARK 500 ALA K 87 -121.61 47.34
REMARK 500 VAL K 188 -71.35 -94.29
REMARK 500 SER K 341 -53.03 -140.58
REMARK 500 GLU L 65 -90.05 -99.83
REMARK 500 ALA L 87 -120.67 48.17
REMARK 500 ARG L 103 12.63 -55.95
REMARK 500 ASP L 104 -133.35 65.10
REMARK 500 GLU L 105 -44.49 -4.84
REMARK 500 ASN L 125 -10.11 72.75
REMARK 500 VAL L 188 -74.28 -92.92
REMARK 500 LEU L 285 94.60 -67.67
REMARK 500 LEU L 337 50.48 -116.69
REMARK 500 SER L 341 -55.11 -139.79
REMARK 500 GLN L 368 2.72 -63.01
REMARK 500 ASP L 369 6.44 -67.00
REMARK 500 GLU P 65 -89.31 -100.11
REMARK 500 ALA P 87 -125.41 55.67
REMARK 500 VAL P 188 -71.62 -93.42
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ACETYL GROUP (ACE): ACETYLATED AMINO TERMINUS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 1421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN C 1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN K 1415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN P 1416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN Q 1412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HSP47-COLLAGEN COMPLEX
REMARK 900 RELATED ID: 4AU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HSP47
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DISORDERED SIDE CHAINS MODELLED AS ALA,GLY
DBREF 3ZHA A 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA B 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA C 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA D 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA E 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA F 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA G 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA H 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA I 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA J 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA K 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA L 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA M 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA N 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA O 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA P 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA Q 36 418 UNP C7C419 C7C419_CANFA 36 418
DBREF 3ZHA R 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA S 0 18 PDB 3ZHA 3ZHA 0 18
DBREF 3ZHA T 0 18 PDB 3ZHA 3ZHA 0 18
SEQADV 3ZHA MET A 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU A 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU A 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS A 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET B 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU B 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU B 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS B 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET C 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU C 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU C 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS C 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET D 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU D 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU D 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS D 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET K 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU K 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU K 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS K 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET L 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU L 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU L 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS L 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET P 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU P 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU P 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS P 426 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA MET Q 35 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA LEU Q 419 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA GLU Q 420 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 421 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 422 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 423 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 424 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 425 UNP C7C419 EXPRESSION TAG
SEQADV 3ZHA HIS Q 426 UNP C7C419 EXPRESSION TAG
SEQRES 1 A 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 A 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 A 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 A 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 A 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 A 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 A 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 A 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 A 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 A 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 A 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 A 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 A 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 A 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 A 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 A 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 A 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 A 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 A 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 A 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 A 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 A 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 A 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 A 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 A 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 A 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 A 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 A 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 A 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 A 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 A 392 HIS HIS
SEQRES 1 B 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 B 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 B 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 B 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 B 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 B 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 B 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 B 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 B 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 B 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 B 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 B 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 B 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 B 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 B 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 B 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 B 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 B 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 B 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 B 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 B 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 B 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 B 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 B 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 B 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 B 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 B 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 B 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 B 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 B 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 B 392 HIS HIS
SEQRES 1 C 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 C 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 C 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 C 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 C 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 C 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 C 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 C 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 C 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 C 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 C 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 C 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 C 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 C 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 C 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 C 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 C 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 C 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 C 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 C 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 C 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 C 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 C 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 C 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 C 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 C 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 C 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 C 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 C 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 C 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 C 392 HIS HIS
SEQRES 1 D 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 D 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 D 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 D 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 D 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 D 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 D 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 D 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 D 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 D 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 D 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 D 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 D 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 D 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 D 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 D 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 D 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 D 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 D 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 D 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 D 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 D 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 D 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 D 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 D 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 D 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 D 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 D 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 D 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 D 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 D 392 HIS HIS
SEQRES 1 E 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 E 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 F 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 F 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 G 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 G 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 H 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 H 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 I 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 I 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 J 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 J 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 K 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 K 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 K 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 K 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 K 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 K 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 K 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 K 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 K 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 K 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 K 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 K 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 K 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 K 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 K 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 K 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 K 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 K 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 K 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 K 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 K 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 K 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 K 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 K 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 K 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 K 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 K 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 K 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 K 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 K 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 K 392 HIS HIS
SEQRES 1 L 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 L 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 L 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 L 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 L 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 L 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 L 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 L 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 L 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 L 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 L 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 L 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 L 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 L 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 L 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 L 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 L 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 L 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 L 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 L 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 L 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 L 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 L 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 L 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 L 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 L 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 L 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 L 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 L 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 L 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 L 392 HIS HIS
SEQRES 1 M 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 M 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 N 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 N 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 O 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 O 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 P 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 P 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 P 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 P 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 P 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 P 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 P 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 P 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 P 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 P 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 P 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 P 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 P 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 P 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 P 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 P 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 P 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 P 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 P 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 P 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 P 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 P 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 P 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 P 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 P 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 P 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 P 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 P 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 P 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 P 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 P 392 HIS HIS
SEQRES 1 Q 392 MET LEU SER PRO LYS ALA ALA THR LEU ALA GLU ARG SER
SEQRES 2 Q 392 ALA GLY LEU ALA PHE SER LEU TYR GLN ALA MET ALA LYS
SEQRES 3 Q 392 ASP GLN ALA VAL GLU ASN ILE LEU LEU SER PRO VAL VAL
SEQRES 4 Q 392 VAL ALA SER SER LEU GLY LEU VAL SER LEU GLY GLY LYS
SEQRES 5 Q 392 ALA THR THR ALA SER GLN ALA LYS ALA VAL LEU SER ALA
SEQRES 6 Q 392 GLU GLN LEU ARG ASP GLU GLU VAL HIS ALA GLY LEU GLY
SEQRES 7 Q 392 GLU LEU LEU ARG SER LEU SER ASN SER THR ALA ARG ASN
SEQRES 8 Q 392 VAL THR TRP LYS LEU GLY SER ARG LEU TYR GLY PRO SER
SEQRES 9 Q 392 SER VAL SER PHE ALA GLU ASP PHE VAL ARG SER SER LYS
SEQRES 10 Q 392 GLN HIS TYR ASN CYS GLU HIS SER LYS ILE ASN PHE ARG
SEQRES 11 Q 392 ASP LYS ARG SER ALA LEU GLN SER ILE ASN GLU TRP ALA
SEQRES 12 Q 392 ALA GLN THR THR ASP GLY LYS LEU PRO GLU VAL THR LYS
SEQRES 13 Q 392 ASP VAL GLU ARG THR ASP GLY ALA LEU LEU VAL ASN ALA
SEQRES 14 Q 392 MET PHE PHE LYS PRO HIS TRP ASP GLU LYS PHE HIS HIS
SEQRES 15 Q 392 LYS MET VAL ASP ASN ARG GLY PHE MET VAL THR ARG SER
SEQRES 16 Q 392 TYR THR VAL GLY VAL THR MET MET HIS ARG THR GLY LEU
SEQRES 17 Q 392 TYR ASN TYR TYR ASP ASP GLU LYS GLU LYS LEU GLN ILE
SEQRES 18 Q 392 VAL GLU MET PRO LEU ALA HIS LYS LEU SER SER LEU ILE
SEQRES 19 Q 392 ILE LEU MET PRO HIS HIS VAL GLU PRO LEU GLU ARG LEU
SEQRES 20 Q 392 GLU LYS LEU LEU THR LYS GLU GLN LEU LYS ILE TRP MET
SEQRES 21 Q 392 GLY LYS MET GLN LYS LYS ALA VAL ALA ILE SER LEU PRO
SEQRES 22 Q 392 LYS GLY VAL VAL GLU VAL THR HIS ASP LEU GLN LYS HIS
SEQRES 23 Q 392 LEU ALA GLY LEU GLY LEU THR GLU ALA ILE ASP LYS ASN
SEQRES 24 Q 392 LYS ALA ASP LEU SER ARG MET SER GLY LYS LYS ASP LEU
SEQRES 25 Q 392 TYR LEU ALA SER VAL PHE HIS ALA THR ALA PHE GLU TRP
SEQRES 26 Q 392 ASP THR GLU GLY ASN PRO PHE ASP GLN ASP ILE TYR GLY
SEQRES 27 Q 392 ARG GLU GLU LEU ARG SER PRO LYS LEU PHE TYR ALA ASP
SEQRES 28 Q 392 HIS PRO PHE ILE PHE LEU VAL ARG ASP THR GLN SER GLY
SEQRES 29 Q 392 SER LEU LEU PHE ILE GLY ARG LEU VAL ARG PRO LYS GLY
SEQRES 30 Q 392 ASP LYS MET ARG ASP GLU LEU LEU GLU HIS HIS HIS HIS
SEQRES 31 Q 392 HIS HIS
SEQRES 1 R 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 R 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 S 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 S 19 PRO PRO GLY PRO PRO NH2
SEQRES 1 T 19 ACE PRO PRO GLY PRO PRO GLY PRO THR GLY PRO ARG GLY
SEQRES 2 T 19 PRO PRO GLY PRO PRO NH2
HET ACE E 0 3
HET ACE F 0 3
HET ACE G 0 3
HET ACE H 0 3
HET ACE I 0 3
HET ACE J 0 3
HET ACE M 0 3
HET ACE N 0 3
HET ACE O 0 3
HET ACE R 0 3
HET ACE S 0 3
HET ACE T 0 3
HET SIN A1421 8
HET SIN C1418 8
HET SIN K1415 8
HET SIN P1416 12
HET SIN Q1412 12
HETNAM ACE ACETYL GROUP
HETNAM SIN SUCCINIC ACID
FORMUL 5 ACE 12(C2 H4 O)
FORMUL 21 SIN 5(C4 H6 O4)
FORMUL 26 HOH *222(H2 O)
HELIX 1 1 SER A 37 ASP A 61 1 25
HELIX 2 2 SER A 70 GLY A 85 1 16
HELIX 3 3 LYS A 86 LEU A 97 1 12
HELIX 4 4 ARG A 103 LEU A 118 1 16
HELIX 5 5 ALA A 143 ASN A 155 1 13
HELIX 6 6 ASP A 165 THR A 181 1 17
HELIX 7 7 ALA A 261 LYS A 263 5 3
HELIX 8 8 LEU A 278 LEU A 285 1 8
HELIX 9 9 THR A 286 MET A 297 1 12
HELIX 10 10 LEU A 317 LEU A 324 1 8
HELIX 11 11 LEU A 326 ASP A 331 1 6
HELIX 12 12 ASP A 367 GLY A 372 5 6
HELIX 13 13 ARG A 373 ARG A 377 5 5
HELIX 14 14 SER B 37 ASP B 61 1 25
HELIX 15 15 SER B 70 GLY B 85 1 16
HELIX 16 16 LYS B 86 LEU B 97 1 12
HELIX 17 17 ARG B 103 LEU B 118 1 16
HELIX 18 18 ALA B 143 ASN B 155 1 13
HELIX 19 19 ASP B 165 THR B 181 1 17
HELIX 20 20 ALA B 261 LYS B 263 5 3
HELIX 21 21 LEU B 278 LEU B 285 1 8
HELIX 22 22 THR B 286 MET B 297 1 12
HELIX 23 23 LEU B 317 LEU B 324 1 8
HELIX 24 24 SER C 37 ASP C 61 1 25
HELIX 25 25 SER C 70 GLY C 85 1 16
HELIX 26 26 LYS C 86 LEU C 97 1 12
HELIX 27 27 ARG C 103 LEU C 118 1 16
HELIX 28 28 ALA C 143 ASN C 155 1 13
HELIX 29 29 ASP C 165 THR C 181 1 17
HELIX 30 30 ALA C 261 LYS C 263 5 3
HELIX 31 31 LEU C 278 LEU C 285 1 8
HELIX 32 32 THR C 286 MET C 297 1 12
HELIX 33 33 LEU C 317 LEU C 324 1 8
HELIX 34 34 LEU C 326 ASP C 331 1 6
HELIX 35 35 ASP C 367 GLY C 372 5 6
HELIX 36 36 SER D 37 ASP D 61 1 25
HELIX 37 37 SER D 70 GLY D 85 1 16
HELIX 38 38 LYS D 86 LEU D 97 1 12
HELIX 39 39 ARG D 103 LEU D 118 1 16
HELIX 40 40 ALA D 143 ASN D 155 1 13
HELIX 41 41 ASP D 165 THR D 181 1 17
HELIX 42 42 ALA D 261 LYS D 263 5 3
HELIX 43 43 LEU D 278 LEU D 285 1 8
HELIX 44 44 THR D 286 MET D 297 1 12
HELIX 45 45 LEU D 317 LEU D 324 1 8
HELIX 46 46 LEU D 326 ASP D 331 1 6
HELIX 47 47 SER K 37 ASP K 61 1 25
HELIX 48 48 SER K 70 GLY K 85 1 16
HELIX 49 49 LYS K 86 LEU K 97 1 12
HELIX 50 50 ARG K 103 LEU K 118 1 16
HELIX 51 51 ALA K 143 ASN K 155 1 13
HELIX 52 52 ASP K 165 THR K 181 1 17
HELIX 53 53 ALA K 261 LYS K 263 5 3
HELIX 54 54 LEU K 278 LEU K 285 1 8
HELIX 55 55 THR K 286 MET K 297 1 12
HELIX 56 56 LEU K 317 LEU K 324 1 8
HELIX 57 57 ASP K 367 ARG K 373 5 7
HELIX 58 58 ARG K 373 ARG K 377 5 5
HELIX 59 59 SER L 37 ASP L 61 1 25
HELIX 60 60 SER L 70 GLY L 84 1 15
HELIX 61 61 LYS L 86 LEU L 97 1 12
HELIX 62 62 GLU L 105 LEU L 118 1 14
HELIX 63 63 ALA L 143 ASN L 155 1 13
HELIX 64 64 ASP L 165 THR L 181 1 17
HELIX 65 65 ALA L 261 LYS L 263 5 3
HELIX 66 66 LEU L 278 LEU L 285 1 8
HELIX 67 67 THR L 286 MET L 297 1 12
HELIX 68 68 LEU L 317 LEU L 324 1 8
HELIX 69 69 LEU L 326 ASP L 331 1 6
HELIX 70 70 SER P 37 ASP P 61 1 25
HELIX 71 71 SER P 70 GLY P 85 1 16
HELIX 72 72 ALA P 87 LEU P 97 1 11
HELIX 73 73 ARG P 103 LEU P 118 1 16
HELIX 74 74 ALA P 143 ASN P 155 1 13
HELIX 75 75 ASP P 165 THR P 181 1 17
HELIX 76 76 ALA P 261 LYS P 263 5 3
HELIX 77 77 LEU P 278 LEU P 285 1 8
HELIX 78 78 THR P 286 MET P 297 1 12
HELIX 79 79 LEU P 317 LEU P 324 1 8
HELIX 80 80 LEU P 326 ASP P 331 1 6
HELIX 81 81 ASP P 367 ARG P 373 5 7
HELIX 82 82 ARG P 373 ARG P 377 5 5
HELIX 83 83 SER Q 37 ASP Q 61 1 25
HELIX 84 84 SER Q 70 GLY Q 85 1 16
HELIX 85 85 LYS Q 86 SER Q 98 1 13
HELIX 86 86 ARG Q 103 LEU Q 118 1 16
HELIX 87 87 ALA Q 143 ASN Q 155 1 13
HELIX 88 88 ASP Q 165 THR Q 181 1 17
HELIX 89 89 ALA Q 261 LYS Q 263 5 3
HELIX 90 90 LEU Q 278 LEU Q 285 1 8
HELIX 91 91 THR Q 286 MET Q 297 1 12
HELIX 92 92 LEU Q 317 LEU Q 324 1 8
SHEET 1 AA11 ILE A 67 LEU A 69 0
SHEET 2 AA11 LEU A 400 LEU A 406 1 O ILE A 403 N LEU A 69
SHEET 3 AA11 PHE A 388 ASP A 394 1 O PHE A 388 N LEU A 406
SHEET 4 AA11 SER A 265 PRO A 272 1 O SER A 266 N ARG A 393
SHEET 5 AA11 LEU A 253 PRO A 259 -1 O GLN A 254 N MET A 271
SHEET 6 AA11 THR A 231 ASP A 248 1 O ASN A 244 N GLU A 257
SHEET 7 AA11 GLN A 298 ASP A 316 -1 O GLN A 298 N TYR A 245
SHEET 8 AA11 LEU A 348 TRP A 359 -1 O HIS A 353 N HIS A 315
SHEET 9 AA11 ALA A 198 LYS A 207 1 O ALA A 198 N ALA A 349
SHEET 10 AA11 THR A 127 PRO A 137 -1 O THR A 127 N LYS A 207
SHEET 11 AA11 CYS A 156 ILE A 161 1 O GLU A 157 N LEU A 134
SHEET 1 AB 7 ILE A 67 LEU A 69 0
SHEET 2 AB 7 LEU A 400 LEU A 406 1 O ILE A 403 N LEU A 69
SHEET 3 AB 7 PHE A 388 ASP A 394 1 O PHE A 388 N LEU A 406
SHEET 4 AB 7 SER A 265 PRO A 272 1 O SER A 266 N ARG A 393
SHEET 5 AB 7 LEU A 253 PRO A 259 -1 O GLN A 254 N MET A 271
SHEET 6 AB 7 THR A 231 ASP A 248 1 O ASN A 244 N GLU A 257
SHEET 7 AB 7 VAL A 219 MET A 225 -1 O ASP A 220 N MET A 236
SHEET 1 AC 2 LYS A 380 TYR A 383 0
SHEET 2 AC 2 GLN A 298 ASP A 316 -1 O ALA A 301 N LYS A 380
SHEET 1 AD 8 ILE A 67 LEU A 69 0
SHEET 2 AD 8 LEU A 400 LEU A 406 1 O ILE A 403 N LEU A 69
SHEET 3 AD 8 PHE A 388 ASP A 394 1 O PHE A 388 N LEU A 406
SHEET 4 AD 8 SER A 265 PRO A 272 1 O SER A 266 N ARG A 393
SHEET 5 AD 8 LEU A 253 PRO A 259 -1 O GLN A 254 N MET A 271
SHEET 6 AD 8 THR A 231 ASP A 248 1 O ASN A 244 N GLU A 257
SHEET 7 AD 8 GLN A 298 ASP A 316 -1 O GLN A 298 N TYR A 245
SHEET 8 AD 8 LYS A 380 TYR A 383 -1 O LYS A 380 N ALA A 303
SHEET 1 BA11 ILE B 67 LEU B 69 0
SHEET 2 BA11 LEU B 400 LEU B 406 1 O ILE B 403 N LEU B 69
SHEET 3 BA11 PHE B 388 ASP B 394 1 O PHE B 388 N LEU B 406
SHEET 4 BA11 SER B 265 PRO B 272 1 O SER B 266 N ARG B 393
SHEET 5 BA11 LEU B 253 PRO B 259 -1 O GLN B 254 N MET B 271
SHEET 6 BA11 THR B 231 ASP B 248 1 O ASN B 244 N GLU B 257
SHEET 7 BA11 GLN B 298 ASP B 316 -1 O GLN B 298 N TYR B 245
SHEET 8 BA11 LEU B 348 TRP B 359 -1 O HIS B 353 N HIS B 315
SHEET 9 BA11 ALA B 198 LYS B 207 1 O ALA B 198 N ALA B 349
SHEET 10 BA11 THR B 127 PRO B 137 -1 O THR B 127 N LYS B 207
SHEET 11 BA11 CYS B 156 ILE B 161 1 O GLU B 157 N LEU B 134
SHEET 1 BB 7 ILE B 67 LEU B 69 0
SHEET 2 BB 7 LEU B 400 LEU B 406 1 O ILE B 403 N LEU B 69
SHEET 3 BB 7 PHE B 388 ASP B 394 1 O PHE B 388 N LEU B 406
SHEET 4 BB 7 SER B 265 PRO B 272 1 O SER B 266 N ARG B 393
SHEET 5 BB 7 LEU B 253 PRO B 259 -1 O GLN B 254 N MET B 271
SHEET 6 BB 7 THR B 231 ASP B 248 1 O ASN B 244 N GLU B 257
SHEET 7 BB 7 VAL B 219 MET B 225 -1 O ASP B 220 N MET B 236
SHEET 1 BC 2 LYS B 380 TYR B 383 0
SHEET 2 BC 2 GLN B 298 ASP B 316 -1 O ALA B 301 N LYS B 380
SHEET 1 BD 8 ILE B 67 LEU B 69 0
SHEET 2 BD 8 LEU B 400 LEU B 406 1 O ILE B 403 N LEU B 69
SHEET 3 BD 8 PHE B 388 ASP B 394 1 O PHE B 388 N LEU B 406
SHEET 4 BD 8 SER B 265 PRO B 272 1 O SER B 266 N ARG B 393
SHEET 5 BD 8 LEU B 253 PRO B 259 -1 O GLN B 254 N MET B 271
SHEET 6 BD 8 THR B 231 ASP B 248 1 O ASN B 244 N GLU B 257
SHEET 7 BD 8 GLN B 298 ASP B 316 -1 O GLN B 298 N TYR B 245
SHEET 8 BD 8 LYS B 380 TYR B 383 -1 O LYS B 380 N ALA B 303
SHEET 1 CA11 ILE C 67 LEU C 69 0
SHEET 2 CA11 LEU C 400 LEU C 406 1 O ILE C 403 N LEU C 69
SHEET 3 CA11 PHE C 388 ASP C 394 1 O PHE C 388 N LEU C 406
SHEET 4 CA11 SER C 265 PRO C 272 1 O SER C 266 N ARG C 393
SHEET 5 CA11 LEU C 253 PRO C 259 -1 O GLN C 254 N MET C 271
SHEET 6 CA11 TYR C 230 ASP C 248 1 O ASN C 244 N GLU C 257
SHEET 7 CA11 GLN C 298 ASP C 316 -1 O GLN C 298 N TYR C 245
SHEET 8 CA11 LEU C 348 TRP C 359 -1 O HIS C 353 N HIS C 315
SHEET 9 CA11 ALA C 198 LYS C 207 1 O ALA C 198 N ALA C 349
SHEET 10 CA11 THR C 127 PRO C 137 -1 O THR C 127 N LYS C 207
SHEET 11 CA11 CYS C 156 ILE C 161 1 O GLU C 157 N LEU C 134
SHEET 1 CB 7 ILE C 67 LEU C 69 0
SHEET 2 CB 7 LEU C 400 LEU C 406 1 O ILE C 403 N LEU C 69
SHEET 3 CB 7 PHE C 388 ASP C 394 1 O PHE C 388 N LEU C 406
SHEET 4 CB 7 SER C 265 PRO C 272 1 O SER C 266 N ARG C 393
SHEET 5 CB 7 LEU C 253 PRO C 259 -1 O GLN C 254 N MET C 271
SHEET 6 CB 7 TYR C 230 ASP C 248 1 O ASN C 244 N GLU C 257
SHEET 7 CB 7 VAL C 219 THR C 227 -1 O ASP C 220 N MET C 236
SHEET 1 CC 2 LYS C 380 TYR C 383 0
SHEET 2 CC 2 GLN C 298 ASP C 316 -1 O ALA C 301 N LYS C 380
SHEET 1 CD 8 ILE C 67 LEU C 69 0
SHEET 2 CD 8 LEU C 400 LEU C 406 1 O ILE C 403 N LEU C 69
SHEET 3 CD 8 PHE C 388 ASP C 394 1 O PHE C 388 N LEU C 406
SHEET 4 CD 8 SER C 265 PRO C 272 1 O SER C 266 N ARG C 393
SHEET 5 CD 8 LEU C 253 PRO C 259 -1 O GLN C 254 N MET C 271
SHEET 6 CD 8 TYR C 230 ASP C 248 1 O ASN C 244 N GLU C 257
SHEET 7 CD 8 GLN C 298 ASP C 316 -1 O GLN C 298 N TYR C 245
SHEET 8 CD 8 LYS C 380 TYR C 383 -1 O LYS C 380 N ALA C 303
SHEET 1 DA11 ILE D 67 LEU D 69 0
SHEET 2 DA11 LEU D 400 LEU D 406 1 O ILE D 403 N LEU D 69
SHEET 3 DA11 PHE D 388 ASP D 394 1 O PHE D 388 N LEU D 406
SHEET 4 DA11 SER D 265 PRO D 272 1 O SER D 266 N ARG D 393
SHEET 5 DA11 LEU D 253 PRO D 259 -1 O GLN D 254 N MET D 271
SHEET 6 DA11 THR D 231 ASP D 248 1 O ASN D 244 N GLU D 257
SHEET 7 DA11 GLN D 298 ASP D 316 -1 O GLN D 298 N TYR D 245
SHEET 8 DA11 LEU D 348 TRP D 359 -1 O HIS D 353 N HIS D 315
SHEET 9 DA11 ALA D 198 LYS D 207 1 O ALA D 198 N ALA D 349
SHEET 10 DA11 THR D 127 PRO D 137 -1 O THR D 127 N LYS D 207
SHEET 11 DA11 CYS D 156 ILE D 161 1 O GLU D 157 N LEU D 134
SHEET 1 DB 7 ILE D 67 LEU D 69 0
SHEET 2 DB 7 LEU D 400 LEU D 406 1 O ILE D 403 N LEU D 69
SHEET 3 DB 7 PHE D 388 ASP D 394 1 O PHE D 388 N LEU D 406
SHEET 4 DB 7 SER D 265 PRO D 272 1 O SER D 266 N ARG D 393
SHEET 5 DB 7 LEU D 253 PRO D 259 -1 O GLN D 254 N MET D 271
SHEET 6 DB 7 THR D 231 ASP D 248 1 O ASN D 244 N GLU D 257
SHEET 7 DB 7 VAL D 219 MET D 225 -1 O ASP D 220 N MET D 236
SHEET 1 DC 2 LYS D 380 TYR D 383 0
SHEET 2 DC 2 GLN D 298 ASP D 316 -1 O ALA D 301 N LYS D 380
SHEET 1 DD 8 ILE D 67 LEU D 69 0
SHEET 2 DD 8 LEU D 400 LEU D 406 1 O ILE D 403 N LEU D 69
SHEET 3 DD 8 PHE D 388 ASP D 394 1 O PHE D 388 N LEU D 406
SHEET 4 DD 8 SER D 265 PRO D 272 1 O SER D 266 N ARG D 393
SHEET 5 DD 8 LEU D 253 PRO D 259 -1 O GLN D 254 N MET D 271
SHEET 6 DD 8 THR D 231 ASP D 248 1 O ASN D 244 N GLU D 257
SHEET 7 DD 8 GLN D 298 ASP D 316 -1 O GLN D 298 N TYR D 245
SHEET 8 DD 8 LYS D 380 TYR D 383 -1 O LYS D 380 N ALA D 303
SHEET 1 KA11 ILE K 67 LEU K 69 0
SHEET 2 KA11 LEU K 400 LEU K 406 1 O ILE K 403 N LEU K 69
SHEET 3 KA11 PHE K 388 ASP K 394 1 O PHE K 388 N LEU K 406
SHEET 4 KA11 SER K 265 PRO K 272 1 O SER K 266 N ARG K 393
SHEET 5 KA11 LEU K 253 PRO K 259 -1 O GLN K 254 N MET K 271
SHEET 6 KA11 THR K 231 ASP K 248 1 O ASN K 244 N GLU K 257
SHEET 7 KA11 GLN K 298 ASP K 316 -1 O GLN K 298 N TYR K 245
SHEET 8 KA11 LEU K 348 TRP K 359 -1 O HIS K 353 N HIS K 315
SHEET 9 KA11 ALA K 198 PHE K 206 1 O ALA K 198 N ALA K 349
SHEET 10 KA11 TRP K 128 PRO K 137 -1 O LYS K 129 N PHE K 205
SHEET 11 KA11 CYS K 156 ILE K 161 1 O GLU K 157 N LEU K 134
SHEET 1 KB 7 ILE K 67 LEU K 69 0
SHEET 2 KB 7 LEU K 400 LEU K 406 1 O ILE K 403 N LEU K 69
SHEET 3 KB 7 PHE K 388 ASP K 394 1 O PHE K 388 N LEU K 406
SHEET 4 KB 7 SER K 265 PRO K 272 1 O SER K 266 N ARG K 393
SHEET 5 KB 7 LEU K 253 PRO K 259 -1 O GLN K 254 N MET K 271
SHEET 6 KB 7 THR K 231 ASP K 248 1 O ASN K 244 N GLU K 257
SHEET 7 KB 7 VAL K 219 MET K 225 -1 O ASP K 220 N MET K 236
SHEET 1 KC 2 LYS K 380 TYR K 383 0
SHEET 2 KC 2 GLN K 298 ASP K 316 -1 O ALA K 301 N LYS K 380
SHEET 1 KD 8 ILE K 67 LEU K 69 0
SHEET 2 KD 8 LEU K 400 LEU K 406 1 O ILE K 403 N LEU K 69
SHEET 3 KD 8 PHE K 388 ASP K 394 1 O PHE K 388 N LEU K 406
SHEET 4 KD 8 SER K 265 PRO K 272 1 O SER K 266 N ARG K 393
SHEET 5 KD 8 LEU K 253 PRO K 259 -1 O GLN K 254 N MET K 271
SHEET 6 KD 8 THR K 231 ASP K 248 1 O ASN K 244 N GLU K 257
SHEET 7 KD 8 GLN K 298 ASP K 316 -1 O GLN K 298 N TYR K 245
SHEET 8 KD 8 LYS K 380 TYR K 383 -1 O LYS K 380 N ALA K 303
SHEET 1 LA11 ILE L 67 LEU L 69 0
SHEET 2 LA11 LEU L 400 LEU L 406 1 O ILE L 403 N LEU L 69
SHEET 3 LA11 PHE L 388 ASP L 394 1 O PHE L 388 N LEU L 406
SHEET 4 LA11 SER L 265 PRO L 272 1 O SER L 266 N ARG L 393
SHEET 5 LA11 LEU L 253 PRO L 259 -1 O GLN L 254 N MET L 271
SHEET 6 LA11 THR L 231 ASP L 248 1 O ASN L 244 N GLU L 257
SHEET 7 LA11 GLN L 298 ASP L 316 -1 O GLN L 298 N TYR L 245
SHEET 8 LA11 LEU L 348 TRP L 359 -1 O HIS L 353 N HIS L 315
SHEET 9 LA11 ALA L 198 LYS L 207 1 O ALA L 198 N ALA L 349
SHEET 10 LA11 THR L 127 PRO L 137 -1 O THR L 127 N LYS L 207
SHEET 11 LA11 CYS L 156 ILE L 161 1 O GLU L 157 N LEU L 134
SHEET 1 LB 7 ILE L 67 LEU L 69 0
SHEET 2 LB 7 LEU L 400 LEU L 406 1 O ILE L 403 N LEU L 69
SHEET 3 LB 7 PHE L 388 ASP L 394 1 O PHE L 388 N LEU L 406
SHEET 4 LB 7 SER L 265 PRO L 272 1 O SER L 266 N ARG L 393
SHEET 5 LB 7 LEU L 253 PRO L 259 -1 O GLN L 254 N MET L 271
SHEET 6 LB 7 THR L 231 ASP L 248 1 O ASN L 244 N GLU L 257
SHEET 7 LB 7 VAL L 219 MET L 225 -1 O ASP L 220 N MET L 236
SHEET 1 LC 2 LYS L 380 TYR L 383 0
SHEET 2 LC 2 GLN L 298 ASP L 316 -1 O ALA L 301 N LYS L 380
SHEET 1 LD 8 ILE L 67 LEU L 69 0
SHEET 2 LD 8 LEU L 400 LEU L 406 1 O ILE L 403 N LEU L 69
SHEET 3 LD 8 PHE L 388 ASP L 394 1 O PHE L 388 N LEU L 406
SHEET 4 LD 8 SER L 265 PRO L 272 1 O SER L 266 N ARG L 393
SHEET 5 LD 8 LEU L 253 PRO L 259 -1 O GLN L 254 N MET L 271
SHEET 6 LD 8 THR L 231 ASP L 248 1 O ASN L 244 N GLU L 257
SHEET 7 LD 8 GLN L 298 ASP L 316 -1 O GLN L 298 N TYR L 245
SHEET 8 LD 8 LYS L 380 TYR L 383 -1 O LYS L 380 N ALA L 303
SHEET 1 PA11 ILE P 67 LEU P 69 0
SHEET 2 PA11 LEU P 400 LEU P 406 1 O ILE P 403 N LEU P 69
SHEET 3 PA11 PHE P 388 ASP P 394 1 O PHE P 388 N LEU P 406
SHEET 4 PA11 SER P 265 PRO P 272 1 O SER P 266 N ARG P 393
SHEET 5 PA11 LEU P 253 PRO P 259 -1 O GLN P 254 N MET P 271
SHEET 6 PA11 THR P 231 ASP P 248 1 O ASN P 244 N GLU P 257
SHEET 7 PA11 GLN P 298 ASP P 316 -1 O GLN P 298 N TYR P 245
SHEET 8 PA11 LEU P 348 TRP P 359 -1 O HIS P 353 N HIS P 315
SHEET 9 PA11 ALA P 198 PHE P 206 1 O ALA P 198 N ALA P 349
SHEET 10 PA11 TRP P 128 PRO P 137 -1 O LYS P 129 N PHE P 205
SHEET 11 PA11 CYS P 156 ILE P 161 1 O GLU P 157 N LEU P 134
SHEET 1 PB 7 ILE P 67 LEU P 69 0
SHEET 2 PB 7 LEU P 400 LEU P 406 1 O ILE P 403 N LEU P 69
SHEET 3 PB 7 PHE P 388 ASP P 394 1 O PHE P 388 N LEU P 406
SHEET 4 PB 7 SER P 265 PRO P 272 1 O SER P 266 N ARG P 393
SHEET 5 PB 7 LEU P 253 PRO P 259 -1 O GLN P 254 N MET P 271
SHEET 6 PB 7 THR P 231 ASP P 248 1 O ASN P 244 N GLU P 257
SHEET 7 PB 7 VAL P 219 MET P 225 -1 O ASP P 220 N MET P 236
SHEET 1 PC 2 LYS P 380 TYR P 383 0
SHEET 2 PC 2 GLN P 298 ASP P 316 -1 O ALA P 301 N LYS P 380
SHEET 1 PD 8 ILE P 67 LEU P 69 0
SHEET 2 PD 8 LEU P 400 LEU P 406 1 O ILE P 403 N LEU P 69
SHEET 3 PD 8 PHE P 388 ASP P 394 1 O PHE P 388 N LEU P 406
SHEET 4 PD 8 SER P 265 PRO P 272 1 O SER P 266 N ARG P 393
SHEET 5 PD 8 LEU P 253 PRO P 259 -1 O GLN P 254 N MET P 271
SHEET 6 PD 8 THR P 231 ASP P 248 1 O ASN P 244 N GLU P 257
SHEET 7 PD 8 GLN P 298 ASP P 316 -1 O GLN P 298 N TYR P 245
SHEET 8 PD 8 LYS P 380 TYR P 383 -1 O LYS P 380 N ALA P 303
SHEET 1 QA11 ILE Q 67 LEU Q 69 0
SHEET 2 QA11 LEU Q 400 LEU Q 406 1 O ILE Q 403 N LEU Q 69
SHEET 3 QA11 PHE Q 388 ASP Q 394 1 O PHE Q 388 N LEU Q 406
SHEET 4 QA11 SER Q 265 PRO Q 272 1 O SER Q 266 N ARG Q 393
SHEET 5 QA11 LEU Q 253 PRO Q 259 -1 O GLN Q 254 N MET Q 271
SHEET 6 QA11 THR Q 231 ASP Q 248 1 O ASN Q 244 N GLU Q 257
SHEET 7 QA11 GLN Q 298 ASP Q 316 -1 O GLN Q 298 N TYR Q 245
SHEET 8 QA11 LEU Q 348 TRP Q 359 -1 O HIS Q 353 N HIS Q 315
SHEET 9 QA11 ALA Q 198 LYS Q 207 1 O ALA Q 198 N ALA Q 349
SHEET 10 QA11 THR Q 127 PRO Q 137 -1 O THR Q 127 N LYS Q 207
SHEET 11 QA11 CYS Q 156 ILE Q 161 1 O GLU Q 157 N LEU Q 134
SHEET 1 QB 7 ILE Q 67 LEU Q 69 0
SHEET 2 QB 7 LEU Q 400 LEU Q 406 1 O ILE Q 403 N LEU Q 69
SHEET 3 QB 7 PHE Q 388 ASP Q 394 1 O PHE Q 388 N LEU Q 406
SHEET 4 QB 7 SER Q 265 PRO Q 272 1 O SER Q 266 N ARG Q 393
SHEET 5 QB 7 LEU Q 253 PRO Q 259 -1 O GLN Q 254 N MET Q 271
SHEET 6 QB 7 THR Q 231 ASP Q 248 1 O ASN Q 244 N GLU Q 257
SHEET 7 QB 7 VAL Q 219 MET Q 225 -1 O ASP Q 220 N MET Q 236
SHEET 1 QC 2 PRO Q 379 TYR Q 383 0
SHEET 2 QC 2 GLN Q 298 ASP Q 316 -1 O ALA Q 301 N LYS Q 380
SHEET 1 QD 8 ILE Q 67 LEU Q 69 0
SHEET 2 QD 8 LEU Q 400 LEU Q 406 1 O ILE Q 403 N LEU Q 69
SHEET 3 QD 8 PHE Q 388 ASP Q 394 1 O PHE Q 388 N LEU Q 406
SHEET 4 QD 8 SER Q 265 PRO Q 272 1 O SER Q 266 N ARG Q 393
SHEET 5 QD 8 LEU Q 253 PRO Q 259 -1 O GLN Q 254 N MET Q 271
SHEET 6 QD 8 THR Q 231 ASP Q 248 1 O ASN Q 244 N GLU Q 257
SHEET 7 QD 8 GLN Q 298 ASP Q 316 -1 O GLN Q 298 N TYR Q 245
SHEET 8 QD 8 PRO Q 379 TYR Q 383 -1 O LYS Q 380 N ALA Q 303
LINK C ACE E 0 N PRO E 1 1555 1555 1.34
LINK C ACE F 0 N PRO F 1 1555 1555 1.34
LINK C ACE G 0 N PRO G 1 1555 1555 1.34
LINK C ACE H 0 N PRO H 1 1555 1555 1.34
LINK C ACE I 0 N PRO I 1 1555 1555 1.34
LINK C ACE J 0 N PRO J 1 1555 1555 1.35
LINK C ACE M 0 N PRO M 1 1555 1555 1.35
LINK C ACE N 0 N PRO N 1 1555 1555 1.34
LINK C ACE O 0 N PRO O 1 1555 1555 1.34
LINK C ACE R 0 N PRO R 1 1555 1555 1.34
LINK C ACE S 0 N PRO S 1 1555 1555 1.34
LINK C ACE T 0 N PRO T 1 1555 1555 1.34
SITE 1 AC1 6 ALA A 63 GLU A 65 ASN A 66 VAL A 313
SITE 2 AC1 6 THR A 314 HIS A 315
SITE 1 AC2 6 ALA C 63 VAL C 64 GLU C 65 ASN C 66
SITE 2 AC2 6 THR C 314 HIS C 315
SITE 1 AC3 6 ALA K 63 GLU K 65 ASN K 66 THR K 314
SITE 2 AC3 6 HIS K 315 HOH K2002
SITE 1 AC4 5 ALA P 63 GLU P 65 ASN P 66 THR P 314
SITE 2 AC4 5 HIS P 315
SITE 1 AC5 7 ALA Q 63 GLU Q 65 ASN Q 66 VAL Q 313
SITE 2 AC5 7 THR Q 314 HIS Q 315 HOH Q2002
CRYST1 102.709 104.905 171.840 90.00 103.71 90.00 P 1 2 1 24
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 0.009736 0.000000 0.002375 0.00000
SCALE2 0.000000 0.009532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005990 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
