HEADER LIGASE 17-APR-15 4ZDI
TITLE CRYSTAL STRUCTURE OF THE M. TUBERCULOSIS CTP SYNTHASE PYRG (APO FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CTP SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: CTP SYNTHETASE,UTP--AMMONIA LIGASE;
COMPND 5 EC: 6.3.4.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 GENE: PYRG, RV1699, MTCI125.21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS CTP SYNTHASE, PYRG, AMIDOTRANSFERASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BELLINZONI,N.BARILONE,P.M.ALZARI
REVDAT 3 10-JAN-24 4ZDI 1 REMARK
REVDAT 2 05-AUG-15 4ZDI 1 JRNL
REVDAT 1 01-JUL-15 4ZDI 0
JRNL AUTH G.MORI,L.R.CHIARELLI,M.ESPOSITO,V.MAKAROV,M.BELLINZONI,
JRNL AUTH 2 R.C.HARTKOORN,G.DEGIACOMI,F.BOLDRIN,S.EKINS,
JRNL AUTH 3 A.L.DE JESUS LOPES RIBEIRO,L.B.MARINO,I.CENTAROVA,
JRNL AUTH 4 Z.SVETLIKOVA,J.BLASKO,E.KAZAKOVA,A.LEPIOSHKIN,N.BARILONE,
JRNL AUTH 5 G.ZANONI,A.PORTA,M.FONDI,R.FANI,A.R.BAULARD,K.MIKUSOVA,
JRNL AUTH 6 P.M.ALZARI,R.MANGANELLI,L.P.DE CARVALHO,G.RICCARDI,S.T.COLE,
JRNL AUTH 7 M.R.PASCA
JRNL TITL THIOPHENECARBOXAMIDE DERIVATIVES ACTIVATED BY ETHA KILL
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS BY INHIBITING THE CTP SYNTHETASE
JRNL TITL 3 PYRG.
JRNL REF CHEM.BIOL. V. 22 917 2015
JRNL REFN ISSN 1074-5521
JRNL PMID 26097035
JRNL DOI 10.1016/J.CHEMBIOL.2015.05.016
REMARK 2
REMARK 2 RESOLUTION. 3.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.1
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) : 3.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 85620
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4288
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) : 3.52
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.62
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6285
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2520
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5962
REMARK 3 BIN R VALUE (WORKING SET) : 0.2516
REMARK 3 BIN FREE R VALUE : 0.2577
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.14
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 323
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 : 30929
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 111.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 28.09450
REMARK 3 B22 (A**2) : 28.09450
REMARK 3 B33 (A**2) : -56.18900
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.810
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.447
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.871
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.871
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 31615 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 43267 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 13921 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 638 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 4834 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 31615 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 4321 ; 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 : 35111 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.89
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.72
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|7 - A|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3830 36.9348 -8.9464
REMARK 3 T TENSOR
REMARK 3 T11: -0.0703 T22: 0.0007
REMARK 3 T33: -0.1523 T12: -0.0019
REMARK 3 T13: 0.1002 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 2.0878 L22: 1.2944
REMARK 3 L33: 2.1669 L12: -0.7453
REMARK 3 L13: 0.4740 L23: 0.2108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: -0.0293 S13: 0.1119
REMARK 3 S21: 0.1014 S22: 0.0882 S23: -0.0941
REMARK 3 S31: 0.0127 S32: 0.0964 S33: -0.1108
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|279 - A|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 64.1252 30.7574 8.6993
REMARK 3 T TENSOR
REMARK 3 T11: 0.0303 T22: 0.0798
REMARK 3 T33: -0.0153 T12: 0.0461
REMARK 3 T13: -0.0732 T23: -0.0844
REMARK 3 L TENSOR
REMARK 3 L11: 0.2528 L22: 0.0000
REMARK 3 L33: 1.8476 L12: -0.6045
REMARK 3 L13: 1.5685 L23: 0.4817
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: -0.0272 S13: -0.0079
REMARK 3 S21: 0.0628 S22: 0.0216 S23: -0.0123
REMARK 3 S31: 0.0130 S32: -0.0140 S33: -0.0257
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|299 - A|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3850 12.5682 -15.2181
REMARK 3 T TENSOR
REMARK 3 T11: -0.1090 T22: 0.0204
REMARK 3 T33: -0.1889 T12: 0.0637
REMARK 3 T13: 0.0213 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 4.5499 L22: 3.0550
REMARK 3 L33: 1.7292 L12: -1.3186
REMARK 3 L13: -1.0512 L23: 1.6759
REMARK 3 S TENSOR
REMARK 3 S11: -0.0408 S12: 0.1380 S13: -0.0676
REMARK 3 S21: -0.0751 S22: 0.0152 S23: -0.0357
REMARK 3 S31: -0.0365 S32: -0.0803 S33: 0.0256
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { B|7 - B|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5417 -32.4548 2.9061
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: -0.0550
REMARK 3 T33: -0.2055 T12: 0.0935
REMARK 3 T13: 0.0914 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.3756 L22: 2.4137
REMARK 3 L33: 0.8717 L12: -0.3942
REMARK 3 L13: -0.4973 L23: -0.4307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: 0.0317 S13: 0.1832
REMARK 3 S21: -0.2621 S22: -0.0884 S23: -0.1762
REMARK 3 S31: 0.1353 S32: 0.0452 S33: 0.0617
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { B|279 - B|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2420 -17.2721 -15.1092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0414 T22: 0.0725
REMARK 3 T33: -0.0149 T12: 0.1163
REMARK 3 T13: 0.1405 T23: 0.0898
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.3656
REMARK 3 L33: 1.7577 L12: 0.0693
REMARK 3 L13: -2.8359 L23: -2.2551
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0368 S13: 0.0182
REMARK 3 S21: -0.0157 S22: 0.0042 S23: -0.0065
REMARK 3 S31: 0.0239 S32: 0.0124 S33: -0.0041
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|299 - B|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6155 -7.0522 -2.8060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0120 T22: -0.0379
REMARK 3 T33: -0.2967 T12: 0.0888
REMARK 3 T13: -0.0128 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 2.7449 L22: 5.0341
REMARK 3 L33: 1.5977 L12: -0.7495
REMARK 3 L13: 0.1081 L23: 0.1841
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: 0.0267 S13: 0.0013
REMARK 3 S21: -0.0928 S22: -0.2153 S23: -0.0574
REMARK 3 S31: 0.1612 S32: -0.0299 S33: 0.1870
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { C|7 - C|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2950 15.5032 35.4329
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.0339
REMARK 3 T33: -0.2964 T12: -0.1433
REMARK 3 T13: 0.0309 T23: 0.0727
REMARK 3 L TENSOR
REMARK 3 L11: 2.9950 L22: 1.9508
REMARK 3 L33: 1.1233 L12: 0.3889
REMARK 3 L13: 0.4354 L23: -0.0898
REMARK 3 S TENSOR
REMARK 3 S11: -0.1340 S12: 0.0728 S13: 0.1545
REMARK 3 S21: -0.1952 S22: 0.3083 S23: -0.0515
REMARK 3 S31: -0.0030 S32: 0.0592 S33: -0.1743
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { C|279 - C|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4080 11.6692 17.8433
REMARK 3 T TENSOR
REMARK 3 T11: 0.1393 T22: 0.0388
REMARK 3 T33: -0.0928 T12: -0.1211
REMARK 3 T13: -0.0775 T23: 0.1438
REMARK 3 L TENSOR
REMARK 3 L11: 0.1317 L22: 0.0000
REMARK 3 L33: 1.7429 L12: -0.0637
REMARK 3 L13: 1.6337 L23: -1.2868
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0242 S13: 0.0010
REMARK 3 S21: -0.0213 S22: 0.0074 S23: 0.0104
REMARK 3 S31: -0.0107 S32: 0.0261 S33: -0.0077
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { C|299 - C|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4023 -9.1736 40.3607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0290 T22: -0.0426
REMARK 3 T33: -0.2639 T12: -0.0787
REMARK 3 T13: 0.0054 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 5.7278 L22: 2.9135
REMARK 3 L33: 1.1584 L12: 1.8171
REMARK 3 L13: -0.6640 L23: -0.9550
REMARK 3 S TENSOR
REMARK 3 S11: -0.1437 S12: -0.0527 S13: -0.1857
REMARK 3 S21: -0.0321 S22: 0.0435 S23: -0.0034
REMARK 3 S31: -0.1764 S32: 0.0390 S33: 0.1002
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { D|7 - D|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5946 24.4391 66.2805
REMARK 3 T TENSOR
REMARK 3 T11: -0.1609 T22: 0.1278
REMARK 3 T33: -0.1880 T12: 0.1520
REMARK 3 T13: -0.0892 T23: -0.1264
REMARK 3 L TENSOR
REMARK 3 L11: 1.1899 L22: 3.4896
REMARK 3 L33: 1.4018 L12: -0.4301
REMARK 3 L13: 0.4871 L23: -0.0773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0672 S12: -0.1058 S13: 0.1127
REMARK 3 S21: -0.0132 S22: 0.1459 S23: -0.2815
REMARK 3 S31: -0.0226 S32: -0.0442 S33: -0.0786
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { D|279 - D|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 83.4438 30.2088 83.0138
REMARK 3 T TENSOR
REMARK 3 T11: 0.0239 T22: 0.0269
REMARK 3 T33: 0.0619 T12: 0.1051
REMARK 3 T13: -0.1134 T23: -0.1397
REMARK 3 L TENSOR
REMARK 3 L11: 0.3700 L22: 0.6019
REMARK 3 L33: 0.7119 L12: 0.5161
REMARK 3 L13: 1.2261 L23: 2.2931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0200 S13: 0.0121
REMARK 3 S21: 0.0435 S22: 0.0072 S23: -0.0188
REMARK 3 S31: -0.0293 S32: -0.0135 S33: -0.0101
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { D|299 - D|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 92.3569 1.2106 73.5752
REMARK 3 T TENSOR
REMARK 3 T11: -0.1661 T22: 0.1113
REMARK 3 T33: -0.2066 T12: 0.1520
REMARK 3 T13: -0.1155 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 3.8502 L22: 3.1175
REMARK 3 L33: 1.5549 L12: -1.2720
REMARK 3 L13: -0.1336 L23: 0.1491
REMARK 3 S TENSOR
REMARK 3 S11: -0.0677 S12: 0.0248 S13: -0.0301
REMARK 3 S21: -0.0460 S22: -0.0279 S23: -0.0680
REMARK 3 S31: -0.0520 S32: -0.1650 S33: 0.0956
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { E|7 - E|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4994 52.5426 65.5275
REMARK 3 T TENSOR
REMARK 3 T11: -0.1655 T22: 0.0804
REMARK 3 T33: -0.1206 T12: 0.1511
REMARK 3 T13: -0.1119 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 1.2251 L22: 3.2057
REMARK 3 L33: 2.0674 L12: 0.0984
REMARK 3 L13: -0.5609 L23: -0.4400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0746 S12: -0.1488 S13: 0.0587
REMARK 3 S21: 0.0926 S22: 0.1829 S23: 0.2343
REMARK 3 S31: 0.1042 S32: -0.0130 S33: -0.1083
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { E|279 - E|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0185 48.8314 83.8902
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.0256
REMARK 3 T33: -0.0039 T12: 0.0785
REMARK 3 T13: 0.0480 T23: 0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 0.1332 L22: 0.0357
REMARK 3 L33: 1.0721 L12: -0.1722
REMARK 3 L13: -1.0794 L23: -1.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.0170 S13: -0.0050
REMARK 3 S21: 0.0408 S22: 0.0032 S23: 0.0100
REMARK 3 S31: 0.0039 S32: 0.0166 S33: -0.0051
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { E|299 - E|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0561 76.4072 71.5567
REMARK 3 T TENSOR
REMARK 3 T11: -0.2072 T22: -0.0340
REMARK 3 T33: 0.0984 T12: 0.1407
REMARK 3 T13: -0.0391 T23: -0.1374
REMARK 3 L TENSOR
REMARK 3 L11: 3.0819 L22: 1.9347
REMARK 3 L33: 1.3825 L12: -0.7816
REMARK 3 L13: 0.2596 L23: -0.4177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0286 S12: -0.0260 S13: -0.0168
REMARK 3 S21: -0.0582 S22: -0.0013 S23: 0.0870
REMARK 3 S31: -0.0303 S32: -0.0024 S33: 0.0299
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: { F|6 - F|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 74.3767 -55.4830 1.7916
REMARK 3 T TENSOR
REMARK 3 T11: -0.0676 T22: -0.1337
REMARK 3 T33: -0.0850 T12: 0.1519
REMARK 3 T13: 0.1461 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.7244 L22: 1.5587
REMARK 3 L33: 1.9018 L12: -0.0010
REMARK 3 L13: 0.6501 L23: 0.6704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: 0.1545 S13: -0.1580
REMARK 3 S21: -0.1309 S22: -0.0702 S23: -0.1403
REMARK 3 S31: -0.0349 S32: -0.0432 S33: 0.0080
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: { F|279 - F|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 68.9356 -72.1675 -15.2071
REMARK 3 T TENSOR
REMARK 3 T11: 0.0327 T22: 0.0551
REMARK 3 T33: 0.0233 T12: 0.1058
REMARK 3 T13: -0.0458 T23: -0.0965
REMARK 3 L TENSOR
REMARK 3 L11: 0.4238 L22: 0.2950
REMARK 3 L33: 1.7274 L12: 0.4485
REMARK 3 L13: 1.3203 L23: 1.0436
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0343 S13: -0.0029
REMARK 3 S21: -0.0261 S22: 0.0053 S23: -0.0017
REMARK 3 S31: -0.0219 S32: -0.0112 S33: -0.0070
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: { F|299 - F|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 97.9416 -81.1464 -5.5571
REMARK 3 T TENSOR
REMARK 3 T11: -0.0707 T22: -0.0807
REMARK 3 T33: -0.0887 T12: 0.1512
REMARK 3 T13: 0.1469 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 2.5991 L22: 4.0424
REMARK 3 L33: 0.5890 L12: -2.5053
REMARK 3 L13: -0.2043 L23: 0.1836
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: 0.0474 S13: 0.0384
REMARK 3 S21: 0.0615 S22: -0.1615 S23: -0.1131
REMARK 3 S31: -0.0663 S32: -0.0741 S33: 0.1189
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: { G|7 - G|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 82.0221 -38.2862 33.1303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: -0.1937
REMARK 3 T33: -0.0277 T12: -0.0722
REMARK 3 T13: 0.1294 T23: -0.0598
REMARK 3 L TENSOR
REMARK 3 L11: 1.6861 L22: 1.6262
REMARK 3 L33: 2.3645 L12: 0.2009
REMARK 3 L13: -0.5214 L23: 0.2197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: -0.1141 S13: 0.0734
REMARK 3 S21: 0.1830 S22: -0.0847 S23: -0.1046
REMARK 3 S31: 0.0118 S32: 0.0107 S33: 0.0565
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: { G|279 - G|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 85.6310 -22.0457 50.6417
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0109
REMARK 3 T33: -0.0002 T12: -0.0321
REMARK 3 T13: 0.0388 T23: -0.0813
REMARK 3 L TENSOR
REMARK 3 L11: 0.0608 L22: 0.2690
REMARK 3 L33: 1.7111 L12: -0.3549
REMARK 3 L13: -1.1099 L23: 0.9668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: -0.0370 S13: -0.0053
REMARK 3 S21: 0.0134 S22: 0.0128 S23: 0.0049
REMARK 3 S31: 0.0269 S32: -0.0185 S33: -0.0138
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: { G|299 - G|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 106.7900 -13.1408 28.8070
REMARK 3 T TENSOR
REMARK 3 T11: -0.0465 T22: -0.1960
REMARK 3 T33: 0.1153 T12: -0.1427
REMARK 3 T13: 0.0068 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 2.2049 L22: 3.6691
REMARK 3 L33: 0.6255 L12: 0.6409
REMARK 3 L13: -0.9324 L23: -1.3351
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.0221 S13: -0.0040
REMARK 3 S21: -0.0610 S22: -0.0658 S23: -0.0860
REMARK 3 S31: 0.0691 S32: -0.0528 S33: 0.0578
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: { H|7 - H|278 }
REMARK 3 ORIGIN FOR THE GROUP (A): 58.5339 62.0513 31.2089
REMARK 3 T TENSOR
REMARK 3 T11: 0.1003 T22: -0.0741
REMARK 3 T33: -0.2678 T12: -0.1520
REMARK 3 T13: -0.1483 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.6745 L22: 1.7421
REMARK 3 L33: 2.8817 L12: 1.9609
REMARK 3 L13: -1.0008 L23: 1.2808
REMARK 3 S TENSOR
REMARK 3 S11: -0.1459 S12: -0.0272 S13: 0.0565
REMARK 3 S21: -0.3089 S22: 0.3711 S23: -0.0797
REMARK 3 S31: -0.1097 S32: -0.1157 S33: -0.2252
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: { H|279 - H|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6073 67.5029 13.1746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0663 T22: 0.0236
REMARK 3 T33: -0.0663 T12: -0.1409
REMARK 3 T13: 0.0166 T23: -0.0797
REMARK 3 L TENSOR
REMARK 3 L11: 0.0166 L22: 0.0000
REMARK 3 L33: 1.4028 L12: 0.6321
REMARK 3 L13: -0.7009 L23: -0.5120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0266 S13: 0.0091
REMARK 3 S21: -0.0243 S22: 0.0095 S23: -0.0188
REMARK 3 S31: -0.0228 S32: -0.0208 S33: -0.0120
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: { H|299 - H|551 }
REMARK 3 ORIGIN FOR THE GROUP (A): 84.3555 85.7130 37.2450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0822 T22: -0.1363
REMARK 3 T33: -0.1946 T12: -0.1520
REMARK 3 T13: -0.0292 T23: -0.1382
REMARK 3 L TENSOR
REMARK 3 L11: 4.3332 L22: 2.0763
REMARK 3 L33: 0.9979 L12: 1.8331
REMARK 3 L13: 0.5354 L23: 0.7563
REMARK 3 S TENSOR
REMARK 3 S11: -0.1137 S12: -0.1448 S13: 0.1151
REMARK 3 S21: -0.1960 S22: 0.1481 S23: -0.0506
REMARK 3 S31: 0.0419 S32: -0.1068 S33: -0.0344
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85758
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.520
REMARK 200 RESOLUTION RANGE LOW (A) : 49.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.99800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 4ZDJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG8000, 200 MM CA ACETATE, 100 MM
REMARK 280 HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 92.02350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 138.03525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.01175
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2458 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39935 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 46.01175
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -46.01175
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 LYS A 3
REMARK 465 HIS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 PRO A 430
REMARK 465 ASP A 431
REMARK 465 GLN A 432
REMARK 465 GLU A 433
REMARK 465 GLU A 434
REMARK 465 ILE A 435
REMARK 465 VAL A 436
REMARK 465 ALA A 437
REMARK 465 GLY A 438
REMARK 465 GLU A 439
REMARK 465 ALA A 440
REMARK 465 ASP A 441
REMARK 465 LEU A 442
REMARK 465 GLY A 443
REMARK 465 GLU A 552
REMARK 465 LEU A 553
REMARK 465 LEU A 554
REMARK 465 PRO A 555
REMARK 465 VAL A 556
REMARK 465 GLU A 557
REMARK 465 ILE A 558
REMARK 465 PRO A 559
REMARK 465 GLU A 560
REMARK 465 ILE A 561
REMARK 465 PRO A 562
REMARK 465 GLU A 563
REMARK 465 HIS A 564
REMARK 465 THR A 565
REMARK 465 PRO A 566
REMARK 465 ASN A 567
REMARK 465 GLY A 568
REMARK 465 SER A 569
REMARK 465 SER A 570
REMARK 465 HIS A 571
REMARK 465 ARG A 572
REMARK 465 ASP A 573
REMARK 465 GLY A 574
REMARK 465 VAL A 575
REMARK 465 GLY A 576
REMARK 465 GLN A 577
REMARK 465 PRO A 578
REMARK 465 LEU A 579
REMARK 465 PRO A 580
REMARK 465 GLU A 581
REMARK 465 PRO A 582
REMARK 465 ALA A 583
REMARK 465 SER A 584
REMARK 465 ARG A 585
REMARK 465 GLY A 586
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 3
REMARK 465 HIS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 PRO B 430
REMARK 465 ASP B 431
REMARK 465 GLN B 432
REMARK 465 GLU B 433
REMARK 465 GLU B 434
REMARK 465 ILE B 435
REMARK 465 VAL B 436
REMARK 465 ALA B 437
REMARK 465 GLY B 438
REMARK 465 GLU B 439
REMARK 465 ALA B 440
REMARK 465 ASP B 441
REMARK 465 LEU B 442
REMARK 465 LEU B 554
REMARK 465 PRO B 555
REMARK 465 VAL B 556
REMARK 465 GLU B 557
REMARK 465 ILE B 558
REMARK 465 PRO B 559
REMARK 465 GLU B 560
REMARK 465 ILE B 561
REMARK 465 PRO B 562
REMARK 465 GLU B 563
REMARK 465 HIS B 564
REMARK 465 THR B 565
REMARK 465 PRO B 566
REMARK 465 ASN B 567
REMARK 465 GLY B 568
REMARK 465 SER B 569
REMARK 465 SER B 570
REMARK 465 HIS B 571
REMARK 465 ARG B 572
REMARK 465 ASP B 573
REMARK 465 GLY B 574
REMARK 465 VAL B 575
REMARK 465 GLY B 576
REMARK 465 GLN B 577
REMARK 465 PRO B 578
REMARK 465 LEU B 579
REMARK 465 PRO B 580
REMARK 465 GLU B 581
REMARK 465 PRO B 582
REMARK 465 ALA B 583
REMARK 465 SER B 584
REMARK 465 ARG B 585
REMARK 465 GLY B 586
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 LYS C 3
REMARK 465 HIS C 4
REMARK 465 PRO C 5
REMARK 465 GLN C 6
REMARK 465 PRO C 430
REMARK 465 ASP C 431
REMARK 465 GLN C 432
REMARK 465 GLU C 433
REMARK 465 GLU C 434
REMARK 465 ILE C 435
REMARK 465 VAL C 436
REMARK 465 ALA C 437
REMARK 465 GLY C 438
REMARK 465 GLU C 439
REMARK 465 ALA C 440
REMARK 465 ASP C 441
REMARK 465 LEU C 442
REMARK 465 GLY C 443
REMARK 465 LEU C 554
REMARK 465 PRO C 555
REMARK 465 VAL C 556
REMARK 465 GLU C 557
REMARK 465 ILE C 558
REMARK 465 PRO C 559
REMARK 465 GLU C 560
REMARK 465 ILE C 561
REMARK 465 PRO C 562
REMARK 465 GLU C 563
REMARK 465 HIS C 564
REMARK 465 THR C 565
REMARK 465 PRO C 566
REMARK 465 ASN C 567
REMARK 465 GLY C 568
REMARK 465 SER C 569
REMARK 465 SER C 570
REMARK 465 HIS C 571
REMARK 465 ARG C 572
REMARK 465 ASP C 573
REMARK 465 GLY C 574
REMARK 465 VAL C 575
REMARK 465 GLY C 576
REMARK 465 GLN C 577
REMARK 465 PRO C 578
REMARK 465 LEU C 579
REMARK 465 PRO C 580
REMARK 465 GLU C 581
REMARK 465 PRO C 582
REMARK 465 ALA C 583
REMARK 465 SER C 584
REMARK 465 ARG C 585
REMARK 465 GLY C 586
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 LYS D 3
REMARK 465 HIS D 4
REMARK 465 PRO D 5
REMARK 465 GLN D 6
REMARK 465 PRO D 430
REMARK 465 ASP D 431
REMARK 465 GLN D 432
REMARK 465 GLU D 433
REMARK 465 GLU D 434
REMARK 465 ILE D 435
REMARK 465 VAL D 436
REMARK 465 ALA D 437
REMARK 465 GLY D 438
REMARK 465 GLU D 439
REMARK 465 ALA D 440
REMARK 465 ASP D 441
REMARK 465 LEU D 442
REMARK 465 GLY D 443
REMARK 465 GLY D 444
REMARK 465 LEU D 553
REMARK 465 LEU D 554
REMARK 465 PRO D 555
REMARK 465 VAL D 556
REMARK 465 GLU D 557
REMARK 465 ILE D 558
REMARK 465 PRO D 559
REMARK 465 GLU D 560
REMARK 465 ILE D 561
REMARK 465 PRO D 562
REMARK 465 GLU D 563
REMARK 465 HIS D 564
REMARK 465 THR D 565
REMARK 465 PRO D 566
REMARK 465 ASN D 567
REMARK 465 GLY D 568
REMARK 465 SER D 569
REMARK 465 SER D 570
REMARK 465 HIS D 571
REMARK 465 ARG D 572
REMARK 465 ASP D 573
REMARK 465 GLY D 574
REMARK 465 VAL D 575
REMARK 465 GLY D 576
REMARK 465 GLN D 577
REMARK 465 PRO D 578
REMARK 465 LEU D 579
REMARK 465 PRO D 580
REMARK 465 GLU D 581
REMARK 465 PRO D 582
REMARK 465 ALA D 583
REMARK 465 SER D 584
REMARK 465 ARG D 585
REMARK 465 GLY D 586
REMARK 465 GLY E 0
REMARK 465 MET E 1
REMARK 465 ARG E 2
REMARK 465 LYS E 3
REMARK 465 HIS E 4
REMARK 465 PRO E 5
REMARK 465 GLN E 6
REMARK 465 PRO E 430
REMARK 465 ASP E 431
REMARK 465 GLN E 432
REMARK 465 GLU E 433
REMARK 465 GLU E 434
REMARK 465 ILE E 435
REMARK 465 VAL E 436
REMARK 465 ALA E 437
REMARK 465 GLY E 438
REMARK 465 GLU E 439
REMARK 465 ALA E 440
REMARK 465 ASP E 441
REMARK 465 LEU E 442
REMARK 465 GLY E 443
REMARK 465 GLY E 444
REMARK 465 GLU E 552
REMARK 465 LEU E 553
REMARK 465 LEU E 554
REMARK 465 PRO E 555
REMARK 465 VAL E 556
REMARK 465 GLU E 557
REMARK 465 ILE E 558
REMARK 465 PRO E 559
REMARK 465 GLU E 560
REMARK 465 ILE E 561
REMARK 465 PRO E 562
REMARK 465 GLU E 563
REMARK 465 HIS E 564
REMARK 465 THR E 565
REMARK 465 PRO E 566
REMARK 465 ASN E 567
REMARK 465 GLY E 568
REMARK 465 SER E 569
REMARK 465 SER E 570
REMARK 465 HIS E 571
REMARK 465 ARG E 572
REMARK 465 ASP E 573
REMARK 465 GLY E 574
REMARK 465 VAL E 575
REMARK 465 GLY E 576
REMARK 465 GLN E 577
REMARK 465 PRO E 578
REMARK 465 LEU E 579
REMARK 465 PRO E 580
REMARK 465 GLU E 581
REMARK 465 PRO E 582
REMARK 465 ALA E 583
REMARK 465 SER E 584
REMARK 465 ARG E 585
REMARK 465 GLY E 586
REMARK 465 GLY F 0
REMARK 465 MET F 1
REMARK 465 ARG F 2
REMARK 465 LYS F 3
REMARK 465 HIS F 4
REMARK 465 PRO F 5
REMARK 465 GLY F 17
REMARK 465 VAL F 18
REMARK 465 ALA F 19
REMARK 465 SER F 20
REMARK 465 SER F 21
REMARK 465 PRO F 430
REMARK 465 ASP F 431
REMARK 465 GLN F 432
REMARK 465 GLU F 433
REMARK 465 GLU F 434
REMARK 465 ILE F 435
REMARK 465 VAL F 436
REMARK 465 ALA F 437
REMARK 465 GLY F 438
REMARK 465 GLU F 439
REMARK 465 ALA F 440
REMARK 465 ASP F 441
REMARK 465 LEU F 442
REMARK 465 GLY F 443
REMARK 465 GLY F 444
REMARK 465 GLU F 552
REMARK 465 LEU F 553
REMARK 465 LEU F 554
REMARK 465 PRO F 555
REMARK 465 VAL F 556
REMARK 465 GLU F 557
REMARK 465 ILE F 558
REMARK 465 PRO F 559
REMARK 465 GLU F 560
REMARK 465 ILE F 561
REMARK 465 PRO F 562
REMARK 465 GLU F 563
REMARK 465 HIS F 564
REMARK 465 THR F 565
REMARK 465 PRO F 566
REMARK 465 ASN F 567
REMARK 465 GLY F 568
REMARK 465 SER F 569
REMARK 465 SER F 570
REMARK 465 HIS F 571
REMARK 465 ARG F 572
REMARK 465 ASP F 573
REMARK 465 GLY F 574
REMARK 465 VAL F 575
REMARK 465 GLY F 576
REMARK 465 GLN F 577
REMARK 465 PRO F 578
REMARK 465 LEU F 579
REMARK 465 PRO F 580
REMARK 465 GLU F 581
REMARK 465 PRO F 582
REMARK 465 ALA F 583
REMARK 465 SER F 584
REMARK 465 ARG F 585
REMARK 465 GLY F 586
REMARK 465 GLY G 0
REMARK 465 MET G 1
REMARK 465 ARG G 2
REMARK 465 LYS G 3
REMARK 465 HIS G 4
REMARK 465 PRO G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 17
REMARK 465 VAL G 18
REMARK 465 ALA G 19
REMARK 465 PRO G 430
REMARK 465 ASP G 431
REMARK 465 GLN G 432
REMARK 465 GLU G 433
REMARK 465 GLU G 434
REMARK 465 ILE G 435
REMARK 465 VAL G 436
REMARK 465 ALA G 437
REMARK 465 GLY G 438
REMARK 465 GLU G 439
REMARK 465 ALA G 440
REMARK 465 ASP G 441
REMARK 465 LEU G 442
REMARK 465 GLY G 443
REMARK 465 GLY G 444
REMARK 465 GLU G 552
REMARK 465 LEU G 553
REMARK 465 LEU G 554
REMARK 465 PRO G 555
REMARK 465 VAL G 556
REMARK 465 GLU G 557
REMARK 465 ILE G 558
REMARK 465 PRO G 559
REMARK 465 GLU G 560
REMARK 465 ILE G 561
REMARK 465 PRO G 562
REMARK 465 GLU G 563
REMARK 465 HIS G 564
REMARK 465 THR G 565
REMARK 465 PRO G 566
REMARK 465 ASN G 567
REMARK 465 GLY G 568
REMARK 465 SER G 569
REMARK 465 SER G 570
REMARK 465 HIS G 571
REMARK 465 ARG G 572
REMARK 465 ASP G 573
REMARK 465 GLY G 574
REMARK 465 VAL G 575
REMARK 465 GLY G 576
REMARK 465 GLN G 577
REMARK 465 PRO G 578
REMARK 465 LEU G 579
REMARK 465 PRO G 580
REMARK 465 GLU G 581
REMARK 465 PRO G 582
REMARK 465 ALA G 583
REMARK 465 SER G 584
REMARK 465 ARG G 585
REMARK 465 GLY G 586
REMARK 465 GLY H 0
REMARK 465 MET H 1
REMARK 465 ARG H 2
REMARK 465 LYS H 3
REMARK 465 HIS H 4
REMARK 465 PRO H 5
REMARK 465 GLN H 6
REMARK 465 VAL H 18
REMARK 465 ALA H 19
REMARK 465 SER H 20
REMARK 465 SER H 21
REMARK 465 LEU H 22
REMARK 465 PRO H 430
REMARK 465 ASP H 431
REMARK 465 GLN H 432
REMARK 465 GLU H 433
REMARK 465 GLU H 434
REMARK 465 ILE H 435
REMARK 465 VAL H 436
REMARK 465 ALA H 437
REMARK 465 GLY H 438
REMARK 465 GLU H 439
REMARK 465 ALA H 440
REMARK 465 ASP H 441
REMARK 465 LEU H 442
REMARK 465 GLY H 443
REMARK 465 GLY H 444
REMARK 465 GLU H 552
REMARK 465 LEU H 553
REMARK 465 LEU H 554
REMARK 465 PRO H 555
REMARK 465 VAL H 556
REMARK 465 GLU H 557
REMARK 465 ILE H 558
REMARK 465 PRO H 559
REMARK 465 GLU H 560
REMARK 465 ILE H 561
REMARK 465 PRO H 562
REMARK 465 GLU H 563
REMARK 465 HIS H 564
REMARK 465 THR H 565
REMARK 465 PRO H 566
REMARK 465 ASN H 567
REMARK 465 GLY H 568
REMARK 465 SER H 569
REMARK 465 SER H 570
REMARK 465 HIS H 571
REMARK 465 ARG H 572
REMARK 465 ASP H 573
REMARK 465 GLY H 574
REMARK 465 VAL H 575
REMARK 465 GLY H 576
REMARK 465 GLN H 577
REMARK 465 PRO H 578
REMARK 465 LEU H 579
REMARK 465 PRO H 580
REMARK 465 GLU H 581
REMARK 465 PRO H 582
REMARK 465 ALA H 583
REMARK 465 SER H 584
REMARK 465 ARG H 585
REMARK 465 GLY H 586
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 THR A 7 OG1 CG2
REMARK 470 VAL A 18 CG1 CG2
REMARK 470 SER A 20 OG
REMARK 470 SER A 21 OG
REMARK 470 SER A 93 OG
REMARK 470 VAL A 105 CG1 CG2
REMARK 470 LEU A 115 CG CD1 CD2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 138 CG CD OE1 NE2
REMARK 470 ASP A 140 CG OD1 OD2
REMARK 470 ASP A 142 CG OD1 OD2
REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 GLN A 163 CG CD OE1 NE2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 LEU A 198 CG CD1 CD2
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 GLN A 204 CG CD OE1 NE2
REMARK 470 ARG A 226 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 LYS A 235 CG CD CE NZ
REMARK 470 ILE A 244 CG1 CG2 CD1
REMARK 470 ILE A 259 CG1 CG2 CD1
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 282 CG OD1 OD2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 TYR A 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 311 CG1 CG2
REMARK 470 SER A 314 OG
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 ARG A 332 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 336 CG CD OE1 OE2
REMARK 470 ASP A 357 CG OD1 OD2
REMARK 470 VAL A 358 CG1 CG2
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 397 CG CD OE1 NE2
REMARK 470 VAL A 400 CG1 CG2
REMARK 470 LEU A 409 CG CD1 CD2
REMARK 470 THR A 410 OG1 CG2
REMARK 470 ASN A 411 CG OD1 ND2
REMARK 470 ILE A 426 CG1 CG2 CD1
REMARK 470 MET A 429 CG SD CE
REMARK 470 GLN A 463 CG CD OE1 NE2
REMARK 470 THR A 468 OG1 CG2
REMARK 470 LYS A 487 CG CD CE NZ
REMARK 470 ARG A 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 514 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 18 CG1 CG2
REMARK 470 SER B 20 OG
REMARK 470 SER B 21 OG
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 SER B 93 OG
REMARK 470 VAL B 121 CG1 CG2
REMARK 470 ILE B 122 CG1 CG2 CD1
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 ARG B 132 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 134 CG CD1 CD2
REMARK 470 GLN B 138 CG CD OE1 NE2
REMARK 470 ASP B 140 CG OD1 OD2
REMARK 470 ASP B 142 CG OD1 OD2
REMARK 470 ARG B 145 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 160 CG1 CG2 CD1
REMARK 470 GLN B 163 CG CD OE1 NE2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 LEU B 198 CG CD1 CD2
REMARK 470 LYS B 199 CG CD CE NZ
REMARK 470 LYS B 201 CG CD CE NZ
REMARK 470 GLN B 204 CG CD OE1 NE2
REMARK 470 ARG B 211 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 232 CG CD1 CD2
REMARK 470 LYS B 235 CG CD CE NZ
REMARK 470 LEU B 238 CG CD1 CD2
REMARK 470 LYS B 261 CG CD CE NZ
REMARK 470 ARG B 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 277 CG OD1 ND2
REMARK 470 ARG B 281 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 292 CG CD1 CD2
REMARK 470 ARG B 293 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 297 CG CD OE1 OE2
REMARK 470 HIS B 299 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 309 CG CD CE NZ
REMARK 470 TYR B 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL B 311 CG1 CG2
REMARK 470 SER B 314 OG
REMARK 470 ARG B 332 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 336 CG CD OE1 OE2
REMARK 470 ASP B 357 CG OD1 OD2
REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2
REMARK 470 THR B 410 OG1 CG2
REMARK 470 ASN B 411 CG OD1 ND2
REMARK 470 GLN B 463 CG CD OE1 NE2
REMARK 470 THR B 468 OG1 CG2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 ARG B 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 514 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 553 CG CD1 CD2
REMARK 470 VAL C 18 CG1 CG2
REMARK 470 SER C 20 OG
REMARK 470 SER C 21 OG
REMARK 470 LEU C 22 CG CD1 CD2
REMARK 470 SER C 93 OG
REMARK 470 GLN C 138 CG CD OE1 NE2
REMARK 470 ASP C 140 CG OD1 OD2
REMARK 470 ASP C 142 CG OD1 OD2
REMARK 470 ARG C 145 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 163 CG CD OE1 NE2
REMARK 470 HIS C 174 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 179 CG CD OE1 OE2
REMARK 470 LEU C 188 CG CD1 CD2
REMARK 470 GLU C 197 CG CD OE1 OE2
REMARK 470 LEU C 198 CG CD1 CD2
REMARK 470 LYS C 199 CG CD CE NZ
REMARK 470 THR C 200 OG1 CG2
REMARK 470 LYS C 201 CG CD CE NZ
REMARK 470 GLN C 204 CG CD OE1 NE2
REMARK 470 HIS C 205 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 211 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 226 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 230 CG CD OE1 OE2
REMARK 470 LYS C 233 CG CD CE NZ
REMARK 470 LYS C 235 CG CD CE NZ
REMARK 470 LEU C 238 CG CD1 CD2
REMARK 470 LYS C 261 CG CD CE NZ
REMARK 470 ARG C 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 275 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 277 CG OD1 ND2
REMARK 470 LEU C 278 CG CD1 CD2
REMARK 470 ARG C 281 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 293 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 297 CG CD OE1 OE2
REMARK 470 HIS C 299 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 300 CG CD OE1 OE2
REMARK 470 LYS C 309 CG CD CE NZ
REMARK 470 TYR C 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL C 311 CG1 CG2
REMARK 470 SER C 314 OG
REMARK 470 LYS C 330 CG CD CE NZ
REMARK 470 ARG C 332 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 334 CG CD CE NZ
REMARK 470 GLU C 346 CG CD OE1 OE2
REMARK 470 ASP C 357 CG OD1 OD2
REMARK 470 ARG C 370 CG CD NE CZ NH1 NH2
REMARK 470 THR C 410 OG1 CG2
REMARK 470 ASN C 411 CG OD1 ND2
REMARK 470 GLN C 463 CG CD OE1 NE2
REMARK 470 GLN C 466 CG CD OE1 NE2
REMARK 470 THR C 468 OG1 CG2
REMARK 470 LYS C 487 CG CD CE NZ
REMARK 470 ARG C 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 514 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 549 CG CD CE NZ
REMARK 470 LEU C 553 CG CD1 CD2
REMARK 470 VAL D 18 CG1 CG2
REMARK 470 SER D 20 OG
REMARK 470 SER D 21 OG
REMARK 470 SER D 93 OG
REMARK 470 GLN D 138 CG CD OE1 NE2
REMARK 470 ASP D 140 CG OD1 OD2
REMARK 470 ASP D 142 CG OD1 OD2
REMARK 470 ARG D 173 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 179 CG CD OE1 OE2
REMARK 470 LEU D 192 CG CD1 CD2
REMARK 470 SER D 195 OG
REMARK 470 LYS D 199 CG CD CE NZ
REMARK 470 LYS D 201 CG CD CE NZ
REMARK 470 GLN D 204 CG CD OE1 NE2
REMARK 470 HIS D 205 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 227 CG OD1 OD2
REMARK 470 GLU D 230 CG CD OE1 OE2
REMARK 470 LEU D 232 CG CD1 CD2
REMARK 470 LYS D 233 CG CD CE NZ
REMARK 470 LYS D 235 CG CD CE NZ
REMARK 470 ARG D 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 274 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 277 CG OD1 ND2
REMARK 470 ARG D 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 309 CG CD CE NZ
REMARK 470 TYR D 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER D 314 OG
REMARK 470 ARG D 332 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 336 CG CD OE1 OE2
REMARK 470 ASP D 357 CG OD1 OD2
REMARK 470 THR D 410 OG1 CG2
REMARK 470 MET D 429 CG SD CE
REMARK 470 GLN D 463 CG CD OE1 NE2
REMARK 470 THR D 468 OG1 CG2
REMARK 470 LYS D 487 CG CD CE NZ
REMARK 470 ARG D 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 514 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 18 CG1 CG2
REMARK 470 SER E 20 OG
REMARK 470 SER E 21 OG
REMARK 470 SER E 93 OG
REMARK 470 LEU E 115 CG CD1 CD2
REMARK 470 GLN E 138 CG CD OE1 NE2
REMARK 470 ASP E 140 CG OD1 OD2
REMARK 470 ASP E 142 CG OD1 OD2
REMARK 470 GLN E 163 CG CD OE1 NE2
REMARK 470 ARG E 173 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 179 CG CD OE1 OE2
REMARK 470 GLU E 197 CG CD OE1 OE2
REMARK 470 LYS E 199 CG CD CE NZ
REMARK 470 LYS E 201 CG CD CE NZ
REMARK 470 GLN E 204 CG CD OE1 NE2
REMARK 470 LYS E 233 CG CD CE NZ
REMARK 470 LYS E 235 CG CD CE NZ
REMARK 470 MET E 239 CG SD CE
REMARK 470 ASP E 241 CG OD1 OD2
REMARK 470 LYS E 261 CG CD CE NZ
REMARK 470 ARG E 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 274 CG CD NE CZ NH1 NH2
REMARK 470 ASN E 277 CG OD1 ND2
REMARK 470 ARG E 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 309 CG CD CE NZ
REMARK 470 TYR E 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL E 311 CG1 CG2
REMARK 470 GLU E 312 CG CD OE1 OE2
REMARK 470 SER E 314 OG
REMARK 470 ARG E 332 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 336 CG CD OE1 OE2
REMARK 470 ASP E 357 CG OD1 OD2
REMARK 470 THR E 410 OG1 CG2
REMARK 470 ASN E 411 CG OD1 ND2
REMARK 470 MET E 429 CG SD CE
REMARK 470 GLN E 463 CG CD OE1 NE2
REMARK 470 THR E 468 OG1 CG2
REMARK 470 SER E 471 OG
REMARK 470 LYS E 487 CG CD CE NZ
REMARK 470 ARG E 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 514 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 6 CG CD OE1 NE2
REMARK 470 LEU F 22 CG CD1 CD2
REMARK 470 LEU F 86 CG CD1 CD2
REMARK 470 ARG F 88 CG CD NE CZ NH1 NH2
REMARK 470 SER F 93 OG
REMARK 470 LEU F 115 CG CD1 CD2
REMARK 470 ASP F 140 CG OD1 OD2
REMARK 470 ASP F 142 CG OD1 OD2
REMARK 470 ASN F 144 CG OD1 ND2
REMARK 470 ARG F 145 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 163 CG CD OE1 NE2
REMARK 470 ARG F 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 179 CG CD OE1 OE2
REMARK 470 LYS F 201 CG CD CE NZ
REMARK 470 GLN F 204 CG CD OE1 NE2
REMARK 470 ARG F 211 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 230 CG CD OE1 OE2
REMARK 470 LEU F 232 CG CD1 CD2
REMARK 470 LYS F 235 CG CD CE NZ
REMARK 470 ASP F 241 CG OD1 OD2
REMARK 470 LYS F 261 CG CD CE NZ
REMARK 470 ARG F 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 274 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 277 CG OD1 ND2
REMARK 470 ARG F 281 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 300 CG CD OE1 OE2
REMARK 470 LYS F 309 CG CD CE NZ
REMARK 470 TYR F 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL F 311 CG1 CG2
REMARK 470 SER F 314 OG
REMARK 470 LYS F 330 CG CD CE NZ
REMARK 470 ARG F 332 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 334 CG CD CE NZ
REMARK 470 GLU F 336 CG CD OE1 OE2
REMARK 470 ASP F 357 CG OD1 OD2
REMARK 470 LEU F 409 CG CD1 CD2
REMARK 470 THR F 410 OG1 CG2
REMARK 470 ASN F 411 CG OD1 ND2
REMARK 470 MET F 429 CG SD CE
REMARK 470 GLN F 463 CG CD OE1 NE2
REMARK 470 THR F 468 OG1 CG2
REMARK 470 LYS F 487 CG CD CE NZ
REMARK 470 ARG F 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 514 CG CD NE CZ NH1 NH2
REMARK 470 HIS F 515 CG ND1 CD2 CE1 NE2
REMARK 470 ARG F 533 CG CD NE CZ NH1 NH2
REMARK 470 SER G 93 OG
REMARK 470 LYS G 108 CG CD CE NZ
REMARK 470 ARG G 111 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 113 CG CD OE1 OE2
REMARK 470 LEU G 115 CG CD1 CD2
REMARK 470 GLN G 138 CG CD OE1 NE2
REMARK 470 ASP G 140 CG OD1 OD2
REMARK 470 ASP G 142 CG OD1 OD2
REMARK 470 ASN G 144 CG OD1 ND2
REMARK 470 GLN G 163 CG CD OE1 NE2
REMARK 470 ARG G 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 179 CG CD OE1 OE2
REMARK 470 LYS G 201 CG CD CE NZ
REMARK 470 GLN G 204 CG CD OE1 NE2
REMARK 470 HIS G 205 CG ND1 CD2 CE1 NE2
REMARK 470 ASN G 234 CG OD1 ND2
REMARK 470 ARG G 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 274 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 277 CG OD1 ND2
REMARK 470 ARG G 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 309 CG CD CE NZ
REMARK 470 TYR G 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL G 311 CG1 CG2
REMARK 470 GLU G 312 CG CD OE1 OE2
REMARK 470 SER G 314 OG
REMARK 470 ARG G 332 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 336 CG CD OE1 OE2
REMARK 470 ASP G 357 CG OD1 OD2
REMARK 470 PHE G 367 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU G 409 CG CD1 CD2
REMARK 470 THR G 410 OG1 CG2
REMARK 470 ASN G 411 CG OD1 ND2
REMARK 470 MET G 429 CG SD CE
REMARK 470 GLN G 463 CG CD OE1 NE2
REMARK 470 THR G 468 OG1 CG2
REMARK 470 LYS G 487 CG CD CE NZ
REMARK 470 ARG G 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 514 CG CD NE CZ NH1 NH2
REMARK 470 HIS G 515 CG ND1 CD2 CE1 NE2
REMARK 470 THR H 7 OG1 CG2
REMARK 470 LYS H 10 CG CD CE NZ
REMARK 470 LYS H 24 CG CD CE NZ
REMARK 470 ARG H 38 CG CD NE CZ NH1 NH2
REMARK 470 SER H 93 OG
REMARK 470 LEU H 115 CG CD1 CD2
REMARK 470 GLN H 138 CG CD OE1 NE2
REMARK 470 ASP H 140 CG OD1 OD2
REMARK 470 ASP H 142 CG OD1 OD2
REMARK 470 ARG H 145 CG CD NE CZ NH1 NH2
REMARK 470 SER H 162 OG
REMARK 470 GLN H 163 CG CD OE1 NE2
REMARK 470 TYR H 175 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG H 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 179 CG CD OE1 OE2
REMARK 470 TYR H 191 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU H 197 CG CD OE1 OE2
REMARK 470 LYS H 201 CG CD CE NZ
REMARK 470 GLN H 204 CG CD OE1 NE2
REMARK 470 HIS H 205 CG ND1 CD2 CE1 NE2
REMARK 470 LEU H 210 CG CD1 CD2
REMARK 470 ARG H 211 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 220 CG CD1 CD2
REMARK 470 ARG H 226 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 230 CG CD OE1 OE2
REMARK 470 LEU H 232 CG CD1 CD2
REMARK 470 LYS H 233 CG CD CE NZ
REMARK 470 ASN H 234 CG OD1 ND2
REMARK 470 LYS H 235 CG CD CE NZ
REMARK 470 VAL H 242 CG1 CG2
REMARK 470 LYS H 261 CG CD CE NZ
REMARK 470 LEU H 263 CG CD1 CD2
REMARK 470 ARG H 265 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 267 CG CD OE1 OE2
REMARK 470 LEU H 268 CG CD1 CD2
REMARK 470 PHE H 271 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL H 272 CG1 CG2
REMARK 470 ARG H 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 275 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 276 CG CD1 CD2
REMARK 470 ASN H 277 CG OD1 ND2
REMARK 470 PHE H 280 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG H 281 CG CD NE CZ NH1 NH2
REMARK 470 VAL H 283 CG1 CG2
REMARK 470 ASP H 290 CG OD1 OD2
REMARK 470 LEU H 292 CG CD1 CD2
REMARK 470 ARG H 293 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 294 CG CD NE CZ NH1 NH2
REMARK 470 HIS H 296 CG ND1 CD2 CE1 NE2
REMARK 470 GLU H 297 CG CD OE1 OE2
REMARK 470 GLU H 300 CG CD OE1 OE2
REMARK 470 LYS H 309 CG CD CE NZ
REMARK 470 TYR H 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL H 311 CG1 CG2
REMARK 470 SER H 314 OG
REMARK 470 GLU H 322 CG CD OE1 OE2
REMARK 470 LEU H 324 CG CD1 CD2
REMARK 470 LYS H 330 CG CD CE NZ
REMARK 470 ARG H 332 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 334 CG CD CE NZ
REMARK 470 GLU H 336 CG CD OE1 OE2
REMARK 470 ILE H 337 CG1 CG2 CD1
REMARK 470 ASP H 357 CG OD1 OD2
REMARK 470 ARG H 370 CG CD NE CZ NH1 NH2
REMARK 470 THR H 410 OG1 CG2
REMARK 470 ASN H 411 CG OD1 ND2
REMARK 470 MET H 429 CG SD CE
REMARK 470 LEU H 448 CG CD1 CD2
REMARK 470 GLN H 463 CG CD OE1 NE2
REMARK 470 THR H 468 OG1 CG2
REMARK 470 GLN H 469 CG CD OE1 NE2
REMARK 470 ARG H 475 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 477 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 487 CG CD CE NZ
REMARK 470 ARG H 494 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 514 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 528 CG CD CE NZ
REMARK 470 VAL H 539 CG1 CG2
REMARK 470 ILE H 546 CG1 CG2 CD1
REMARK 470 LYS H 549 CG CD CE NZ
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 VAL A 18 -102.04 56.59
REMARK 500 HIS A 124 -54.06 -29.06
REMARK 500 GLU A 312 -60.19 64.92
REMARK 500 CYS A 393 -86.90 51.73
REMARK 500 ARG A 475 74.91 -162.36
REMARK 500 VAL B 18 -101.49 55.94
REMARK 500 PRO B 55 0.59 -69.69
REMARK 500 LEU B 115 80.80 45.24
REMARK 500 GLU B 312 -48.46 73.07
REMARK 500 LEU B 313 105.94 -57.74
REMARK 500 CYS B 393 -87.02 51.17
REMARK 500 ARG B 475 67.24 -161.57
REMARK 500 VAL C 18 -101.64 55.88
REMARK 500 LEU C 115 83.15 48.16
REMARK 500 GLU C 312 -38.39 66.50
REMARK 500 CYS C 393 -86.87 51.50
REMARK 500 ASP C 458 3.03 55.64
REMARK 500 ARG C 475 76.72 -162.03
REMARK 500 VAL D 18 -101.78 56.31
REMARK 500 PRO D 55 5.22 -68.65
REMARK 500 LEU D 115 82.40 49.44
REMARK 500 GLU D 312 -9.14 70.49
REMARK 500 CYS D 393 -86.83 51.64
REMARK 500 ASP D 420 30.50 -94.05
REMARK 500 ARG D 475 76.00 -162.00
REMARK 500 VAL E 18 -102.25 56.29
REMARK 500 LEU E 115 82.42 49.33
REMARK 500 GLU E 312 -22.29 69.06
REMARK 500 CYS E 393 -86.72 51.63
REMARK 500 ARG E 475 76.25 -162.27
REMARK 500 LEU F 115 83.56 48.12
REMARK 500 GLU F 312 -44.98 71.51
REMARK 500 LEU F 313 98.44 -65.08
REMARK 500 CYS F 393 -86.80 51.52
REMARK 500 ARG F 475 75.86 -161.95
REMARK 500 LEU G 115 88.41 52.18
REMARK 500 GLU G 312 -25.95 71.29
REMARK 500 CYS G 393 -86.64 51.59
REMARK 500 LEU G 409 86.41 -68.22
REMARK 500 ARG G 475 75.86 -162.17
REMARK 500 LEU H 115 83.88 49.59
REMARK 500 GLU H 312 -16.76 73.59
REMARK 500 CYS H 393 -86.68 51.67
REMARK 500 ARG H 475 65.02 -163.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 76 OD1
REMARK 620 2 ASP F 76 OD2 40.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 601
DBREF 4ZDI A 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI B 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI C 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI D 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI E 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI F 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI G 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDI H 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
SEQADV 4ZDI GLY A 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY B 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY C 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY D 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY E 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY F 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY G 0 UNP P9WHK7 EXPRESSION TAG
SEQADV 4ZDI GLY H 0 UNP P9WHK7 EXPRESSION TAG
SEQRES 1 A 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 A 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 A 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 A 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 A 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 A 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 A 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 A 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 A 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 A 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 A 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 A 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 A 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 A 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 A 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 A 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 A 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 A 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 A 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 A 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 A 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 A 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 A 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 A 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 A 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 A 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 A 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 A 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 A 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 A 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 A 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 A 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 A 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 A 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 A 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 A 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 A 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 A 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 A 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 A 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 A 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 A 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 A 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 A 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 A 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 A 587 ARG GLY
SEQRES 1 B 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 B 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 B 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 B 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 B 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 B 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 B 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 B 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 B 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 B 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 B 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 B 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 B 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 B 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 B 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 B 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 B 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 B 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 B 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 B 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 B 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 B 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 B 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 B 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 B 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 B 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 B 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 B 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 B 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 B 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 B 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 B 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 B 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 B 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 B 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 B 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 B 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 B 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 B 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 B 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 B 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 B 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 B 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 B 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 B 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 B 587 ARG GLY
SEQRES 1 C 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 C 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 C 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 C 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 C 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 C 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 C 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 C 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 C 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 C 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 C 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 C 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 C 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 C 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 C 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 C 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 C 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 C 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 C 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 C 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 C 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 C 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 C 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 C 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 C 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 C 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 C 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 C 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 C 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 C 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 C 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 C 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 C 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 C 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 C 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 C 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 C 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 C 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 C 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 C 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 C 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 C 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 C 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 C 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 C 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 C 587 ARG GLY
SEQRES 1 D 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 D 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 D 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 D 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 D 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 D 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 D 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 D 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 D 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 D 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 D 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 D 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 D 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 D 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 D 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 D 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 D 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 D 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 D 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 D 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 D 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 D 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 D 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 D 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 D 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 D 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 D 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 D 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 D 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 D 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 D 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 D 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 D 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 D 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 D 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 D 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 D 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 D 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 D 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 D 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 D 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 D 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 D 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 D 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 D 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 D 587 ARG GLY
SEQRES 1 E 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 E 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 E 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 E 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 E 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 E 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 E 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 E 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 E 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 E 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 E 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 E 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 E 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 E 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 E 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 E 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 E 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 E 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 E 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 E 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 E 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 E 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 E 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 E 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 E 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 E 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 E 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 E 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 E 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 E 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 E 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 E 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 E 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 E 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 E 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 E 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 E 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 E 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 E 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 E 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 E 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 E 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 E 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 E 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 E 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 E 587 ARG GLY
SEQRES 1 F 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 F 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 F 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 F 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 F 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 F 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 F 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 F 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 F 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 F 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 F 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 F 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 F 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 F 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 F 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 F 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 F 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 F 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 F 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 F 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 F 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 F 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 F 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 F 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 F 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 F 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 F 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 F 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 F 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 F 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 F 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 F 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 F 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 F 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 F 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 F 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 F 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 F 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 F 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 F 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 F 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 F 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 F 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 F 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 F 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 F 587 ARG GLY
SEQRES 1 G 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 G 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 G 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 G 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 G 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 G 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 G 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 G 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 G 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 G 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 G 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 G 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 G 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 G 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 G 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 G 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 G 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 G 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 G 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 G 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 G 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 G 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 G 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 G 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 G 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 G 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 G 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 G 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 G 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 G 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 G 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 G 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 G 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 G 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 G 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 G 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 G 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 G 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 G 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 G 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 G 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 G 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 G 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 G 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 G 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 G 587 ARG GLY
SEQRES 1 H 587 GLY MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU
SEQRES 2 H 587 PHE VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY
SEQRES 3 H 587 LEU THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG
SEQRES 4 H 587 GLY LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU
SEQRES 5 H 587 ASN VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY
SEQRES 6 H 587 GLU VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU
SEQRES 7 H 587 ASP VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU
SEQRES 8 H 587 PRO GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER
SEQRES 9 H 587 THR VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY
SEQRES 10 H 587 ASP THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE
SEQRES 11 H 587 LYS ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP
SEQRES 12 H 587 GLY ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY
SEQRES 13 H 587 THR VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA
SEQRES 14 H 587 ALA ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL
SEQRES 15 H 587 PHE PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO
SEQRES 16 H 587 SER GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL
SEQRES 17 H 587 ALA ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU
SEQRES 18 H 587 ILE LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS
SEQRES 19 H 587 ASN LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY
SEQRES 20 H 587 VAL ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE
SEQRES 21 H 587 PRO LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL
SEQRES 22 H 587 VAL ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP
SEQRES 23 H 587 THR GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO
SEQRES 24 H 587 HIS GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL
SEQRES 25 H 587 GLU LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU
SEQRES 26 H 587 ARG ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE
SEQRES 27 H 587 CYS TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY
SEQRES 28 H 587 ALA ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE
SEQRES 29 H 587 PRO GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE
SEQRES 30 H 587 GLY ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL
SEQRES 31 H 587 LEU GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU
SEQRES 32 H 587 ALA ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA
SEQRES 33 H 587 GLU PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR
SEQRES 34 H 587 MET PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP
SEQRES 35 H 587 LEU GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL
SEQRES 36 H 587 LEU GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR
SEQRES 37 H 587 THR GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL
SEQRES 38 H 587 ASN ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU
SEQRES 39 H 587 ARG PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU
SEQRES 40 H 587 PHE VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL
SEQRES 41 H 587 GLY THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR
SEQRES 42 H 587 ARG PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA
SEQRES 43 H 587 ILE ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE
SEQRES 44 H 587 PRO GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS
SEQRES 45 H 587 ARG ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER
SEQRES 46 H 587 ARG GLY
HET CA A 601 1
HET CA B 601 1
HET CA C 601 1
HET CA D 601 1
HET CA E 601 1
HET CA F 601 1
HET CA G 601 1
HET CA H 601 1
HETNAM CA CALCIUM ION
FORMUL 9 CA 8(CA 2+)
HELIX 1 AA1 GLY A 23 ARG A 38 1 16
HELIX 2 AA2 ASN A 59 GLY A 64 1 6
HELIX 3 AA3 LEU A 77 ASP A 87 1 11
HELIX 4 AA4 PRO A 91 SER A 93 5 3
HELIX 5 AA5 THR A 98 GLY A 112 1 15
HELIX 6 AA6 PRO A 123 ALA A 135 1 13
HELIX 7 AA7 SER A 162 GLY A 177 1 16
HELIX 8 AA8 THR A 200 ILE A 213 1 14
HELIX 9 AA9 PRO A 229 CYS A 240 1 12
HELIX 10 AB1 ASP A 243 ASP A 245 5 3
HELIX 11 AB2 ASP A 258 GLU A 266 1 9
HELIX 12 AB3 GLU A 267 ASN A 277 1 11
HELIX 13 AB4 TRP A 285 GLU A 297 1 13
HELIX 14 AB5 SER A 314 ALA A 316 5 3
HELIX 15 AB6 TYR A 317 HIS A 331 1 15
HELIX 16 AB7 ASP A 343 GLU A 346 5 4
HELIX 17 AB8 THR A 347 LEU A 355 1 9
HELIX 18 AB9 ILE A 372 GLY A 386 1 15
HELIX 19 AC1 CYS A 393 GLY A 408 1 16
HELIX 20 AC2 SER A 459 GLN A 466 1 8
HELIX 21 AC3 TYR A 484 ALA A 489 1 6
HELIX 22 AC4 GLU A 490 GLY A 492 5 3
HELIX 23 AC5 HIS A 524 LYS A 528 5 5
HELIX 24 AC6 HIS A 535 ALA A 550 1 16
HELIX 25 AC7 GLY B 23 ARG B 38 1 16
HELIX 26 AC8 ASP B 54 MET B 58 5 5
HELIX 27 AC9 ASN B 59 GLY B 64 1 6
HELIX 28 AD1 LEU B 77 ASP B 87 1 11
HELIX 29 AD2 PRO B 91 SER B 93 5 3
HELIX 30 AD3 THR B 98 GLY B 112 1 15
HELIX 31 AD4 PRO B 123 ALA B 135 1 13
HELIX 32 AD5 SER B 162 GLY B 177 1 16
HELIX 33 AD6 THR B 200 ILE B 213 1 14
HELIX 34 AD7 PRO B 229 ASP B 241 1 13
HELIX 35 AD8 ASP B 243 ASP B 245 5 3
HELIX 36 AD9 ASP B 258 GLU B 266 1 9
HELIX 37 AE1 GLU B 267 ASN B 277 1 11
HELIX 38 AE2 TRP B 285 GLU B 297 1 13
HELIX 39 AE3 SER B 314 ALA B 316 5 3
HELIX 40 AE4 TYR B 317 HIS B 331 1 15
HELIX 41 AE5 ASP B 343 GLU B 346 5 4
HELIX 42 AE6 THR B 347 LEU B 355 1 9
HELIX 43 AE7 ILE B 372 GLY B 386 1 15
HELIX 44 AE8 CYS B 393 GLY B 408 1 16
HELIX 45 AE9 SER B 459 GLN B 466 1 8
HELIX 46 AF1 TYR B 484 ALA B 489 1 6
HELIX 47 AF2 GLU B 490 GLY B 492 5 3
HELIX 48 AF3 HIS B 524 LYS B 528 5 5
HELIX 49 AF4 HIS B 535 GLY B 551 1 17
HELIX 50 AF5 GLY C 23 ARG C 38 1 16
HELIX 51 AF6 ASP C 54 MET C 58 5 5
HELIX 52 AF7 ASN C 59 GLY C 64 1 6
HELIX 53 AF8 LEU C 77 ASP C 87 1 11
HELIX 54 AF9 PRO C 91 SER C 93 5 3
HELIX 55 AG1 THR C 98 ARG C 111 1 14
HELIX 56 AG2 PRO C 123 ALA C 135 1 13
HELIX 57 AG3 SER C 162 GLY C 177 1 16
HELIX 58 AG4 THR C 200 ILE C 213 1 14
HELIX 59 AG5 PRO C 229 ASP C 241 1 13
HELIX 60 AG6 ASP C 243 ASP C 245 5 3
HELIX 61 AG7 ASP C 258 GLU C 266 1 9
HELIX 62 AG8 GLU C 267 ASN C 277 1 11
HELIX 63 AG9 TRP C 285 GLU C 297 1 13
HELIX 64 AH1 LEU C 313 ALA C 316 5 4
HELIX 65 AH2 TYR C 317 HIS C 331 1 15
HELIX 66 AH3 ASP C 343 GLU C 346 5 4
HELIX 67 AH4 THR C 347 LEU C 355 1 9
HELIX 68 AH5 ILE C 372 GLY C 386 1 15
HELIX 69 AH6 CYS C 393 GLY C 408 1 16
HELIX 70 AH7 SER C 459 GLN C 466 1 8
HELIX 71 AH8 TYR C 484 ALA C 489 1 6
HELIX 72 AH9 GLU C 490 GLY C 492 5 3
HELIX 73 AI1 HIS C 524 LYS C 528 5 5
HELIX 74 AI2 HIS C 535 ALA C 550 1 16
HELIX 75 AI3 GLY D 23 ARG D 38 1 16
HELIX 76 AI4 ASP D 54 MET D 58 5 5
HELIX 77 AI5 ASN D 59 GLY D 64 1 6
HELIX 78 AI6 LEU D 77 ASP D 87 1 11
HELIX 79 AI7 PRO D 91 SER D 93 5 3
HELIX 80 AI8 THR D 98 GLY D 112 1 15
HELIX 81 AI9 PRO D 123 ALA D 135 1 13
HELIX 82 AJ1 SER D 162 GLY D 177 1 16
HELIX 83 AJ2 THR D 200 ILE D 213 1 14
HELIX 84 AJ3 PRO D 229 CYS D 240 1 12
HELIX 85 AJ4 ASP D 243 ASP D 245 5 3
HELIX 86 AJ5 ASP D 258 GLU D 266 1 9
HELIX 87 AJ6 GLU D 267 ASN D 277 1 11
HELIX 88 AJ7 TRP D 285 GLU D 297 1 13
HELIX 89 AJ8 SER D 314 ALA D 316 5 3
HELIX 90 AJ9 TYR D 317 HIS D 331 1 15
HELIX 91 AK1 ASP D 343 GLU D 346 5 4
HELIX 92 AK2 THR D 347 LEU D 355 1 9
HELIX 93 AK3 ILE D 372 GLY D 386 1 15
HELIX 94 AK4 CYS D 393 GLY D 408 1 16
HELIX 95 AK5 SER D 459 GLN D 466 1 8
HELIX 96 AK6 TYR D 484 ALA D 489 1 6
HELIX 97 AK7 GLU D 490 GLY D 492 5 3
HELIX 98 AK8 HIS D 524 LYS D 528 5 5
HELIX 99 AK9 HIS D 535 ALA D 550 1 16
HELIX 100 AL1 GLY E 23 ARG E 38 1 16
HELIX 101 AL2 ASP E 54 MET E 58 5 5
HELIX 102 AL3 ASN E 59 GLY E 64 1 6
HELIX 103 AL4 LEU E 77 ASP E 87 1 11
HELIX 104 AL5 PRO E 91 SER E 93 5 3
HELIX 105 AL6 THR E 98 GLY E 112 1 15
HELIX 106 AL7 PRO E 123 ALA E 135 1 13
HELIX 107 AL8 MET E 136 GLN E 138 5 3
HELIX 108 AL9 SER E 162 GLY E 177 1 16
HELIX 109 AM1 THR E 200 ILE E 213 1 14
HELIX 110 AM2 PRO E 229 CYS E 240 1 12
HELIX 111 AM3 ASP E 243 ASP E 245 5 3
HELIX 112 AM4 ASP E 258 GLU E 266 1 9
HELIX 113 AM5 GLU E 267 ASN E 277 1 11
HELIX 114 AM6 TRP E 285 GLU E 297 1 13
HELIX 115 AM7 SER E 314 ALA E 316 5 3
HELIX 116 AM8 TYR E 317 HIS E 331 1 15
HELIX 117 AM9 ASP E 343 GLU E 346 5 4
HELIX 118 AN1 THR E 347 LEU E 355 1 9
HELIX 119 AN2 ILE E 372 GLY E 386 1 15
HELIX 120 AN3 CYS E 393 GLY E 408 1 16
HELIX 121 AN4 SER E 459 GLN E 466 1 8
HELIX 122 AN5 TYR E 484 ALA E 489 1 6
HELIX 123 AN6 GLU E 490 GLY E 492 5 3
HELIX 124 AN7 HIS E 524 LYS E 528 5 5
HELIX 125 AN8 HIS E 535 ALA E 550 1 16
HELIX 126 AN9 GLY F 23 ARG F 38 1 16
HELIX 127 AO1 ASP F 54 MET F 58 5 5
HELIX 128 AO2 ASN F 59 GLY F 64 1 6
HELIX 129 AO3 LEU F 77 ASP F 87 1 11
HELIX 130 AO4 PRO F 91 SER F 93 5 3
HELIX 131 AO5 THR F 98 GLY F 112 1 15
HELIX 132 AO6 PRO F 123 ALA F 135 1 13
HELIX 133 AO7 SER F 162 GLY F 177 1 16
HELIX 134 AO8 THR F 200 ILE F 213 1 14
HELIX 135 AO9 PRO F 229 CYS F 240 1 12
HELIX 136 AP1 ASP F 243 ASP F 245 5 3
HELIX 137 AP2 ASP F 258 GLU F 266 1 9
HELIX 138 AP3 GLU F 267 ASN F 277 1 11
HELIX 139 AP4 TRP F 285 GLU F 297 1 13
HELIX 140 AP5 LEU F 313 ALA F 316 5 4
HELIX 141 AP6 TYR F 317 HIS F 331 1 15
HELIX 142 AP7 ASP F 343 GLU F 346 5 4
HELIX 143 AP8 THR F 347 LEU F 355 1 9
HELIX 144 AP9 ILE F 372 GLY F 386 1 15
HELIX 145 AQ1 CYS F 393 GLY F 408 1 16
HELIX 146 AQ2 SER F 459 GLN F 466 1 8
HELIX 147 AQ3 TYR F 484 ALA F 489 1 6
HELIX 148 AQ4 GLU F 490 GLY F 492 5 3
HELIX 149 AQ5 HIS F 524 LYS F 528 5 5
HELIX 150 AQ6 HIS F 535 ALA F 550 1 16
HELIX 151 AQ7 GLY G 23 ARG G 38 1 16
HELIX 152 AQ8 ASN G 59 GLY G 64 1 6
HELIX 153 AQ9 LEU G 77 ASP G 87 1 11
HELIX 154 AR1 PRO G 91 SER G 93 5 3
HELIX 155 AR2 THR G 98 ARG G 111 1 14
HELIX 156 AR3 PRO G 123 ALA G 135 1 13
HELIX 157 AR4 SER G 162 GLY G 177 1 16
HELIX 158 AR5 THR G 200 ILE G 213 1 14
HELIX 159 AR6 PRO G 229 ASP G 241 1 13
HELIX 160 AR7 ASP G 243 ASP G 245 5 3
HELIX 161 AR8 ASP G 258 GLU G 266 1 9
HELIX 162 AR9 GLU G 267 ASN G 277 1 11
HELIX 163 AS1 TRP G 285 GLU G 297 1 13
HELIX 164 AS2 SER G 314 ALA G 316 5 3
HELIX 165 AS3 TYR G 317 HIS G 331 1 15
HELIX 166 AS4 ASP G 343 GLU G 346 5 4
HELIX 167 AS5 THR G 347 LEU G 355 1 9
HELIX 168 AS6 ILE G 372 GLY G 386 1 15
HELIX 169 AS7 CYS G 393 GLY G 408 1 16
HELIX 170 AS8 SER G 459 GLN G 466 1 8
HELIX 171 AS9 TYR G 484 ALA G 489 1 6
HELIX 172 AT1 GLU G 490 GLY G 492 5 3
HELIX 173 AT2 HIS G 524 LYS G 528 5 5
HELIX 174 AT3 HIS G 535 ALA G 550 1 16
HELIX 175 AT4 LYS H 24 ARG H 38 1 15
HELIX 176 AT5 ASN H 59 GLY H 64 1 6
HELIX 177 AT6 LEU H 77 ASP H 87 1 11
HELIX 178 AT7 PRO H 91 SER H 93 5 3
HELIX 179 AT8 THR H 98 GLY H 112 1 15
HELIX 180 AT9 PRO H 123 ALA H 135 1 13
HELIX 181 AU1 SER H 162 GLY H 177 1 16
HELIX 182 AU2 THR H 200 ILE H 213 1 14
HELIX 183 AU3 PRO H 229 ASP H 241 1 13
HELIX 184 AU4 ASP H 243 ASP H 245 5 3
HELIX 185 AU5 ASP H 258 GLU H 266 1 9
HELIX 186 AU6 GLU H 267 ASN H 277 1 11
HELIX 187 AU7 TRP H 285 GLU H 297 1 13
HELIX 188 AU8 TYR H 317 HIS H 331 1 15
HELIX 189 AU9 ASP H 343 GLU H 346 5 4
HELIX 190 AV1 THR H 347 LEU H 355 1 9
HELIX 191 AV2 ILE H 372 GLY H 386 1 15
HELIX 192 AV3 CYS H 393 GLY H 408 1 16
HELIX 193 AV4 SER H 459 GLN H 466 1 8
HELIX 194 AV5 TYR H 484 ALA H 489 1 6
HELIX 195 AV6 GLU H 490 GLY H 492 5 3
HELIX 196 AV7 HIS H 524 LYS H 528 5 5
HELIX 197 AV8 HIS H 535 ALA H 550 1 16
SHEET 1 AA1 7 ASN A 95 THR A 97 0
SHEET 2 AA1 7 VAL A 42 ASP A 48 1 N LYS A 46 O VAL A 96
SHEET 3 AA1 7 VAL A 148 THR A 156 1 O GLU A 152 N GLN A 45
SHEET 4 AA1 7 LYS A 10 GLY A 16 1 N LEU A 12 O THR A 151
SHEET 5 AA1 7 VAL A 181 LEU A 188 1 O LEU A 184 N PHE A 13
SHEET 6 AA1 7 ALA A 219 CYS A 224 1 O ILE A 221 N SER A 187
SHEET 7 AA1 7 VAL A 247 PRO A 251 1 O ILE A 248 N LEU A 220
SHEET 1 AA2 2 PHE A 67 VAL A 68 0
SHEET 2 AA2 2 GLU A 74 THR A 75 -1 O THR A 75 N PHE A 67
SHEET 1 AA311 ALA A 333 ALA A 341 0
SHEET 2 AA311 GLU A 300 GLY A 308 1 N GLU A 300 O LYS A 334
SHEET 3 AA311 GLY A 360 ILE A 363 1 O GLY A 360 N ALA A 305
SHEET 4 AA311 VAL A 389 LEU A 392 1 O LEU A 392 N ILE A 363
SHEET 5 AA311 VAL A 518 THR A 521 1 O THR A 521 N GLY A 391
SHEET 6 AA311 VAL A 505 GLU A 509 -1 N VAL A 508 O GLY A 520
SHEET 7 AA311 ARG A 494 THR A 498 -1 N ARG A 494 O GLU A 509
SHEET 8 AA311 THR A 445 LEU A 455 -1 N VAL A 454 O THR A 498
SHEET 9 AA311 GLN A 469 VAL A 480 -1 O HIS A 476 N ARG A 447
SHEET 10 AA311 ASP A 423 MET A 429 -1 N ALA A 427 O GLU A 479
SHEET 11 AA311 ALA A 412 SER A 414 1 N ASN A 413 O ASP A 423
SHEET 1 AA4 7 ASN B 95 THR B 97 0
SHEET 2 AA4 7 VAL B 42 ASP B 48 1 N ASP B 48 O VAL B 96
SHEET 3 AA4 7 VAL B 148 THR B 156 1 O GLU B 152 N LEU B 47
SHEET 4 AA4 7 LYS B 10 GLY B 16 1 N LEU B 12 O THR B 151
SHEET 5 AA4 7 VAL B 181 LEU B 188 1 O LEU B 184 N PHE B 13
SHEET 6 AA4 7 ALA B 219 CYS B 224 1 O ILE B 221 N SER B 187
SHEET 7 AA4 7 VAL B 247 PRO B 251 1 O ILE B 248 N LEU B 220
SHEET 1 AA5 2 PHE B 67 VAL B 68 0
SHEET 2 AA5 2 GLU B 74 THR B 75 -1 O THR B 75 N PHE B 67
SHEET 1 AA6 9 ALA B 333 ALA B 341 0
SHEET 2 AA6 9 GLU B 300 GLY B 308 1 N GLU B 300 O LYS B 334
SHEET 3 AA6 9 GLY B 360 ILE B 363 1 O GLY B 360 N ALA B 305
SHEET 4 AA6 9 VAL B 389 LEU B 392 1 O LEU B 392 N ILE B 363
SHEET 5 AA6 9 VAL B 518 THR B 521 1 O THR B 521 N GLY B 391
SHEET 6 AA6 9 VAL B 505 GLU B 509 -1 N VAL B 508 O GLY B 520
SHEET 7 AA6 9 ARG B 494 THR B 498 -1 N ARG B 494 O GLU B 509
SHEET 8 AA6 9 ARG B 447 LEU B 455 -1 N VAL B 454 O THR B 498
SHEET 9 AA6 9 GLN B 469 HIS B 476 -1 O HIS B 476 N ARG B 447
SHEET 1 AA7 3 ALA B 412 SER B 414 0
SHEET 2 AA7 3 ASP B 423 THR B 428 1 O ASP B 423 N ASN B 413
SHEET 3 AA7 3 TYR B 478 VAL B 480 -1 O GLU B 479 N ALA B 427
SHEET 1 AA8 7 ASN C 95 THR C 97 0
SHEET 2 AA8 7 VAL C 42 ASP C 48 1 N ASP C 48 O VAL C 96
SHEET 3 AA8 7 VAL C 148 THR C 156 1 O GLU C 152 N LEU C 47
SHEET 4 AA8 7 LYS C 10 GLY C 16 1 N LEU C 12 O THR C 151
SHEET 5 AA8 7 VAL C 181 LEU C 188 1 O LEU C 184 N PHE C 13
SHEET 6 AA8 7 ALA C 219 CYS C 224 1 O ILE C 221 N SER C 187
SHEET 7 AA8 7 VAL C 247 PRO C 251 1 O ILE C 248 N LEU C 220
SHEET 1 AA9 2 PHE C 67 VAL C 68 0
SHEET 2 AA9 2 GLU C 74 THR C 75 -1 O THR C 75 N PHE C 67
SHEET 1 AB1 9 ALA C 333 ALA C 341 0
SHEET 2 AB1 9 GLU C 300 GLY C 308 1 N GLU C 300 O LYS C 334
SHEET 3 AB1 9 GLY C 360 ILE C 363 1 O GLY C 360 N ALA C 305
SHEET 4 AB1 9 VAL C 389 LEU C 392 1 O LEU C 392 N ILE C 363
SHEET 5 AB1 9 VAL C 518 THR C 521 1 O VAL C 519 N VAL C 389
SHEET 6 AB1 9 VAL C 505 GLU C 509 -1 N VAL C 508 O GLY C 520
SHEET 7 AB1 9 ARG C 494 THR C 498 -1 N ARG C 494 O GLU C 509
SHEET 8 AB1 9 ARG C 447 LEU C 455 -1 N VAL C 454 O THR C 498
SHEET 9 AB1 9 GLN C 469 HIS C 476 -1 O HIS C 476 N ARG C 447
SHEET 1 AB2 3 ALA C 412 SER C 414 0
SHEET 2 AB2 3 ASP C 423 ALA C 427 1 O ASP C 423 N ASN C 413
SHEET 3 AB2 3 GLU C 479 VAL C 480 -1 O GLU C 479 N ALA C 427
SHEET 1 AB3 7 ASN D 95 THR D 97 0
SHEET 2 AB3 7 VAL D 42 ASP D 48 1 N ASP D 48 O VAL D 96
SHEET 3 AB3 7 VAL D 148 THR D 156 1 O GLU D 152 N LEU D 47
SHEET 4 AB3 7 LYS D 10 GLY D 16 1 N LEU D 12 O THR D 151
SHEET 5 AB3 7 VAL D 181 LEU D 188 1 O LEU D 184 N PHE D 13
SHEET 6 AB3 7 ALA D 219 CYS D 224 1 O ILE D 221 N SER D 187
SHEET 7 AB3 7 VAL D 247 PRO D 251 1 O ILE D 248 N LEU D 220
SHEET 1 AB4 2 PHE D 67 VAL D 68 0
SHEET 2 AB4 2 GLU D 74 THR D 75 -1 O THR D 75 N PHE D 67
SHEET 1 AB5 2 TYR D 191 LEU D 192 0
SHEET 2 AB5 2 GLU D 197 LEU D 198 -1 O GLU D 197 N LEU D 192
SHEET 1 AB611 ALA D 333 ALA D 341 0
SHEET 2 AB611 GLU D 300 GLY D 308 1 N GLU D 300 O LYS D 334
SHEET 3 AB611 GLY D 360 ILE D 363 1 O GLY D 360 N ALA D 305
SHEET 4 AB611 VAL D 389 LEU D 392 1 O LEU D 392 N ILE D 363
SHEET 5 AB611 VAL D 518 THR D 521 1 O THR D 521 N GLY D 391
SHEET 6 AB611 VAL D 505 GLU D 509 -1 N VAL D 508 O GLY D 520
SHEET 7 AB611 ARG D 494 THR D 498 -1 N ARG D 494 O GLU D 509
SHEET 8 AB611 MET D 446 LEU D 455 -1 N VAL D 454 O THR D 498
SHEET 9 AB611 GLN D 469 VAL D 480 -1 O HIS D 476 N ARG D 447
SHEET 10 AB611 ASP D 423 MET D 429 -1 N ALA D 427 O GLU D 479
SHEET 11 AB611 ALA D 412 SER D 414 1 N ASN D 413 O ASP D 423
SHEET 1 AB7 7 ASN E 95 THR E 97 0
SHEET 2 AB7 7 VAL E 42 ASP E 48 1 N ASP E 48 O VAL E 96
SHEET 3 AB7 7 VAL E 148 THR E 156 1 O GLU E 152 N LEU E 47
SHEET 4 AB7 7 LYS E 10 GLY E 16 1 N LEU E 12 O THR E 151
SHEET 5 AB7 7 VAL E 181 LEU E 188 1 O LEU E 184 N PHE E 13
SHEET 6 AB7 7 ALA E 219 CYS E 224 1 O ILE E 221 N SER E 187
SHEET 7 AB7 7 VAL E 247 PRO E 251 1 O ILE E 248 N LEU E 220
SHEET 1 AB8 2 PHE E 67 VAL E 68 0
SHEET 2 AB8 2 GLU E 74 THR E 75 -1 O THR E 75 N PHE E 67
SHEET 1 AB911 ALA E 333 ALA E 341 0
SHEET 2 AB911 GLU E 300 GLY E 308 1 N GLU E 300 O LYS E 334
SHEET 3 AB911 GLY E 360 ILE E 363 1 O GLY E 360 N ALA E 305
SHEET 4 AB911 VAL E 389 LEU E 392 1 O LEU E 392 N ILE E 363
SHEET 5 AB911 VAL E 518 THR E 521 1 O THR E 521 N GLY E 391
SHEET 6 AB911 VAL E 505 GLU E 509 -1 N VAL E 508 O GLY E 520
SHEET 7 AB911 ARG E 494 THR E 498 -1 N ARG E 494 O GLU E 509
SHEET 8 AB911 MET E 446 LEU E 455 -1 N VAL E 454 O THR E 498
SHEET 9 AB911 GLN E 469 VAL E 480 -1 O HIS E 476 N ARG E 447
SHEET 10 AB911 ASP E 423 MET E 429 -1 N ALA E 427 O GLU E 479
SHEET 11 AB911 ALA E 412 SER E 414 1 N ASN E 413 O ASP E 423
SHEET 1 AC1 7 ASN F 95 THR F 97 0
SHEET 2 AC1 7 VAL F 42 ASP F 48 1 N ASP F 48 O VAL F 96
SHEET 3 AC1 7 VAL F 148 ILE F 153 1 O GLU F 152 N LEU F 47
SHEET 4 AC1 7 LYS F 10 SER F 15 1 N LEU F 12 O THR F 151
SHEET 5 AC1 7 VAL F 181 LEU F 188 1 O LEU F 184 N PHE F 13
SHEET 6 AC1 7 ALA F 219 CYS F 224 1 O ILE F 221 N SER F 187
SHEET 7 AC1 7 VAL F 247 PRO F 251 1 O ILE F 248 N LEU F 220
SHEET 1 AC2 2 PHE F 67 VAL F 68 0
SHEET 2 AC2 2 GLU F 74 THR F 75 -1 O THR F 75 N PHE F 67
SHEET 1 AC311 ALA F 333 ALA F 341 0
SHEET 2 AC311 GLU F 300 GLY F 308 1 N GLU F 300 O LYS F 334
SHEET 3 AC311 GLY F 360 ILE F 363 1 O GLY F 360 N ALA F 305
SHEET 4 AC311 VAL F 389 LEU F 392 1 O LEU F 392 N ILE F 363
SHEET 5 AC311 VAL F 518 THR F 521 1 O THR F 521 N GLY F 391
SHEET 6 AC311 VAL F 505 GLU F 509 -1 N VAL F 508 O GLY F 520
SHEET 7 AC311 ARG F 494 THR F 498 -1 N ARG F 494 O GLU F 509
SHEET 8 AC311 MET F 446 LEU F 455 -1 N VAL F 454 O THR F 498
SHEET 9 AC311 GLN F 469 VAL F 480 -1 O HIS F 476 N ARG F 447
SHEET 10 AC311 ASP F 423 MET F 429 -1 N ALA F 427 O GLU F 479
SHEET 11 AC311 ALA F 412 SER F 414 1 N ASN F 413 O ASP F 423
SHEET 1 AC4 7 ASN G 95 THR G 97 0
SHEET 2 AC4 7 VAL G 42 ASP G 48 1 N ASP G 48 O VAL G 96
SHEET 3 AC4 7 VAL G 148 THR G 156 1 O GLU G 152 N LEU G 47
SHEET 4 AC4 7 LYS G 10 GLY G 16 1 N LEU G 12 O THR G 151
SHEET 5 AC4 7 VAL G 181 LEU G 188 1 O LEU G 184 N PHE G 13
SHEET 6 AC4 7 ALA G 219 CYS G 224 1 O ILE G 221 N SER G 187
SHEET 7 AC4 7 VAL G 247 PRO G 251 1 O ILE G 248 N LEU G 220
SHEET 1 AC5 2 PHE G 67 VAL G 68 0
SHEET 2 AC5 2 GLU G 74 THR G 75 -1 O THR G 75 N PHE G 67
SHEET 1 AC611 ALA G 333 ALA G 341 0
SHEET 2 AC611 GLU G 300 GLY G 308 1 N GLU G 300 O LYS G 334
SHEET 3 AC611 GLY G 360 ILE G 363 1 O GLY G 360 N ALA G 305
SHEET 4 AC611 VAL G 389 LEU G 392 1 O LEU G 392 N ILE G 363
SHEET 5 AC611 VAL G 518 THR G 521 1 O THR G 521 N GLY G 391
SHEET 6 AC611 VAL G 505 GLU G 509 -1 N VAL G 508 O GLY G 520
SHEET 7 AC611 ARG G 494 THR G 498 -1 N ARG G 494 O GLU G 509
SHEET 8 AC611 MET G 446 LEU G 455 -1 N VAL G 454 O THR G 498
SHEET 9 AC611 GLN G 469 VAL G 480 -1 O HIS G 476 N ARG G 447
SHEET 10 AC611 PRO G 424 MET G 429 -1 N ALA G 427 O GLU G 479
SHEET 11 AC611 ASN G 413 SER G 414 1 N ASN G 413 O VAL G 425
SHEET 1 AC7 7 ASN H 95 THR H 97 0
SHEET 2 AC7 7 VAL H 42 ASP H 48 1 N ASP H 48 O VAL H 96
SHEET 3 AC7 7 VAL H 148 THR H 156 1 O GLU H 152 N LEU H 47
SHEET 4 AC7 7 LYS H 10 GLY H 16 1 N VAL H 14 O ILE H 153
SHEET 5 AC7 7 VAL H 181 LEU H 188 1 O LEU H 184 N PHE H 13
SHEET 6 AC7 7 ALA H 219 CYS H 224 1 O ILE H 221 N SER H 187
SHEET 7 AC7 7 VAL H 247 PRO H 251 1 O ILE H 248 N LEU H 220
SHEET 1 AC8 2 PHE H 67 VAL H 68 0
SHEET 2 AC8 2 GLU H 74 THR H 75 -1 O THR H 75 N PHE H 67
SHEET 1 AC911 ALA H 333 ALA H 341 0
SHEET 2 AC911 GLU H 300 GLY H 308 1 N GLU H 300 O LYS H 334
SHEET 3 AC911 GLY H 360 ILE H 363 1 O GLY H 360 N ALA H 305
SHEET 4 AC911 VAL H 389 LEU H 392 1 O LEU H 392 N ILE H 363
SHEET 5 AC911 VAL H 518 THR H 521 1 O THR H 521 N GLY H 391
SHEET 6 AC911 VAL H 505 GLU H 509 -1 N VAL H 508 O GLY H 520
SHEET 7 AC911 ARG H 494 THR H 498 -1 N ARG H 494 O GLU H 509
SHEET 8 AC911 MET H 446 LEU H 455 -1 N VAL H 454 O THR H 498
SHEET 9 AC911 GLN H 469 VAL H 480 -1 O HIS H 476 N ARG H 447
SHEET 10 AC911 ASP H 423 MET H 429 -1 N ALA H 427 O GLU H 479
SHEET 11 AC911 ALA H 412 SER H 414 1 N ASN H 413 O ASP H 423
LINK OD1 ASP D 76 CA CA D 601 1555 1555 3.11
LINK OD2 ASP E 76 CA CA E 601 1555 1555 3.17
LINK OD1 ASP F 76 CA CA F 601 1555 1555 3.20
LINK OD2 ASP F 76 CA CA F 601 1555 1555 3.18
CISPEP 1 ILE A 122 PRO A 123 0 6.71
CISPEP 2 ILE B 122 PRO B 123 0 8.60
CISPEP 3 ILE C 122 PRO C 123 0 6.32
CISPEP 4 ILE D 122 PRO D 123 0 6.83
CISPEP 5 ILE E 122 PRO E 123 0 5.48
CISPEP 6 ILE F 122 PRO F 123 0 6.59
CISPEP 7 ILE G 122 PRO G 123 0 6.36
CISPEP 8 ILE H 122 PRO H 123 0 5.06
SITE 1 AC1 3 HIS A 63 ASP A 76 LEU A 77
SITE 1 AC2 3 HIS B 63 ASP B 76 LEU B 77
SITE 1 AC3 3 HIS C 63 ASP C 76 LEU C 77
SITE 1 AC4 3 HIS D 63 ASP D 76 LEU D 77
SITE 1 AC5 2 ASP E 76 LEU E 77
SITE 1 AC6 1 ASP F 76
SITE 1 AC7 3 HIS G 63 ASP G 76 LEU G 77
SITE 1 AC8 2 ASP H 76 LEU H 77
CRYST1 196.826 196.826 184.047 90.00 90.00 90.00 P 43 32
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 0.005081 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005081 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005433 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
