HEADER DNA BINDING PROTEIN/DNA 28-OCT-13 4NE1
TITLE HUMAN MHF1 MHF2 DNA COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (26-MER);
COMPND 3 CHAIN: E, O, s, u;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (26-MER);
COMPND 7 CHAIN: F, P, t, v;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: CENTROMERE PROTEIN S;
COMPND 11 CHAIN: C, G, A, I, J, K, Q, R, S, T, Y, a, c, e, f, g, k, l, m, n;
COMPND 12 SYNONYM: CENP-S, APOPTOSIS-INDUCING TAF9-LIKE DOMAIN-CONTAINING
COMPND 13 PROTEIN 1, FANCM-INTERACTING HISTONE FOLD PROTEIN 1, FANCONI ANEMIA-
COMPND 14 ASSOCIATED POLYPEPTIDE OF 16 KDA;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: CENTROMERE PROTEIN X;
COMPND 18 CHAIN: D, H, B, L, M, N, U, V, W, X, Z, b, d, h, i, j, o, p, q, r;
COMPND 19 SYNONYM: CENP-X, FANCM-INTERACTING HISTONE FOLD PROTEIN 2, FANCONI
COMPND 20 ANEMIA-ASSOCIATED POLYPEPTIDE OF 10 KDA, RETINOIC ACID-INDUCIBLE GENE
COMPND 21 D9 PROTEIN HOMOLOG, STIMULATED BY RETINOIC ACID GENE 13 PROTEIN
COMPND 22 HOMOLOG;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 8 ORGANISM_TAXID: 32630;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: APITD1, CENPS, FAAP16, MHF1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 ROSSETTA 2;
SOURCE 17 MOL_ID: 4;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: STRA13, CENPX, FAAP10, MHF2;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: BL21 ROSSETTA 2
KEYWDS HISTONE FOLD, DNA REPAIR, GENOME MAINTENANCE, FANCONI ANEMIA, FANCM,
KEYWDS 2 NUCLEUS, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.ZHAO,D.SARO,A.SACHPATZIDIS,P.SUNG,Y.XIONG
REVDAT 4 28-FEB-24 4NE1 1 REMARK
REVDAT 3 29-JAN-20 4NE1 1 REMARK
REVDAT 2 22-JAN-20 4NE1 1 REMARK SEQADV
REVDAT 1 22-JAN-14 4NE1 0
JRNL AUTH Q.ZHAO,D.SARO,A.SACHPATZIDIS,T.R.SINGH,D.SCHLINGMAN,
JRNL AUTH 2 X.F.ZHENG,A.MACK,M.S.TSAI,S.MOCHRIE,L.REGAN,A.R.MEETEI,
JRNL AUTH 3 P.SUNG,Y.XIONG
JRNL TITL THE MHF COMPLEX SENSES BRANCHED DNA BY BINDING A PAIR OF
JRNL TITL 2 CROSSOVER DNA DUPLEXES.
JRNL REF NAT COMMUN V. 5 2987 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 24390579
JRNL DOI 10.1038/NCOMMS3987
REMARK 2
REMARK 2 RESOLUTION. 6.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 6.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 112.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 18329
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) : 0.267
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 824
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 6.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 6.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1247
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 27467
REMARK 3 NUCLEIC ACID ATOMS : 4264
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 363.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -49.05000
REMARK 3 B22 (A**2) : -49.05000
REMARK 3 B33 (A**2) : 98.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.558
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.597
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 385.496
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 32635 ; 0.010 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 44727 ; 1.461 ; 1.845
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3428 ; 6.321 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1328 ;36.788 ;24.307
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5600 ;20.846 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 228 ;18.563 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5024 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22332 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 4
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.452
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -K, -H, -L
REMARK 3 TWIN FRACTION : 0.032
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.022
REMARK 3 TWIN DOMAIN : 4
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.495
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 48
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 14 C 106
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9950 -34.6344 -11.4197
REMARK 3 T TENSOR
REMARK 3 T11: 2.4704 T22: 2.2662
REMARK 3 T33: 2.1149 T12: -0.0430
REMARK 3 T13: -0.3332 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 4.3063 L22: 0.1521
REMARK 3 L33: 1.0692 L12: 0.1925
REMARK 3 L13: -1.5852 L23: -0.2959
REMARK 3 S TENSOR
REMARK 3 S11: 1.6452 S12: 0.0310 S13: 0.8051
REMARK 3 S21: 0.0832 S22: -0.5752 S23: 0.3268
REMARK 3 S31: -0.9277 S32: 0.4787 S33: -1.0700
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 8 D 81
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8186 -38.9636 -12.1730
REMARK 3 T TENSOR
REMARK 3 T11: 2.2581 T22: 1.8948
REMARK 3 T33: 1.7030 T12: 0.1472
REMARK 3 T13: 0.1503 T23: 0.5043
REMARK 3 L TENSOR
REMARK 3 L11: 3.1789 L22: 0.0637
REMARK 3 L33: 1.6268 L12: 0.1366
REMARK 3 L13: 2.1423 L23: 0.0033
REMARK 3 S TENSOR
REMARK 3 S11: -0.6795 S12: 1.3388 S13: 0.4960
REMARK 3 S21: -0.1753 S22: -0.0875 S23: -0.2483
REMARK 3 S31: -0.4901 S32: 1.2632 S33: 0.7670
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 14 G 106
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4963 -54.4558 -6.8397
REMARK 3 T TENSOR
REMARK 3 T11: 1.8037 T22: 2.0082
REMARK 3 T33: 1.5977 T12: -0.1057
REMARK 3 T13: 0.1909 T23: -0.5268
REMARK 3 L TENSOR
REMARK 3 L11: 0.5506 L22: 1.4539
REMARK 3 L33: 0.8027 L12: 0.7366
REMARK 3 L13: 0.5337 L23: 0.8488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.0627 S13: 0.6832
REMARK 3 S21: 0.7928 S22: -0.8917 S23: 1.2120
REMARK 3 S31: -0.1701 S32: -0.4861 S33: 0.8424
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 8 H 81
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9088 -57.8616 -6.5867
REMARK 3 T TENSOR
REMARK 3 T11: 1.3908 T22: 1.0289
REMARK 3 T33: 0.6275 T12: -0.0903
REMARK 3 T13: 0.0212 T23: 0.2060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5752 L22: 8.6631
REMARK 3 L33: 12.1765 L12: -1.9121
REMARK 3 L13: -2.1492 L23: 10.1327
REMARK 3 S TENSOR
REMARK 3 S11: -0.1458 S12: 0.5411 S13: -0.0231
REMARK 3 S21: 0.7880 S22: -0.6780 S23: 0.5319
REMARK 3 S31: 0.3444 S32: -0.5901 S33: 0.8238
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 106
REMARK 3 ORIGIN FOR THE GROUP (A): 41.1077 -96.7986 -5.5505
REMARK 3 T TENSOR
REMARK 3 T11: 1.0568 T22: 1.4356
REMARK 3 T33: 1.4169 T12: -0.0343
REMARK 3 T13: 0.3890 T23: 0.3056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0834 L22: 6.3257
REMARK 3 L33: 4.4090 L12: 0.0704
REMARK 3 L13: 0.0582 L23: 5.2092
REMARK 3 S TENSOR
REMARK 3 S11: 0.2114 S12: 0.0221 S13: 0.1247
REMARK 3 S21: 0.2869 S22: -0.1730 S23: 0.2557
REMARK 3 S31: 0.3061 S32: 0.0872 S33: -0.0384
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 81
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2601 -92.8378 -4.1828
REMARK 3 T TENSOR
REMARK 3 T11: 1.2561 T22: 1.2310
REMARK 3 T33: 1.4073 T12: 0.0871
REMARK 3 T13: 0.0456 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 8.5279 L22: 4.4672
REMARK 3 L33: 0.4900 L12: 5.9404
REMARK 3 L13: 0.1920 L23: 0.4634
REMARK 3 S TENSOR
REMARK 3 S11: 0.1986 S12: 0.1586 S13: 1.1154
REMARK 3 S21: 0.6199 S22: -0.3519 S23: 1.0515
REMARK 3 S31: 0.7465 S32: -0.0546 S33: 0.1534
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 14 I 118
REMARK 3 ORIGIN FOR THE GROUP (A): 81.1618 52.0700 40.8734
REMARK 3 T TENSOR
REMARK 3 T11: 1.5062 T22: 1.5351
REMARK 3 T33: 0.7841 T12: -0.1126
REMARK 3 T13: -0.0925 T23: -0.3456
REMARK 3 L TENSOR
REMARK 3 L11: 8.5356 L22: 3.4599
REMARK 3 L33: 1.4865 L12: 0.3181
REMARK 3 L13: -1.5561 L23: -2.0873
REMARK 3 S TENSOR
REMARK 3 S11: -0.3256 S12: -1.0701 S13: 1.2884
REMARK 3 S21: -0.7561 S22: -0.0526 S23: -1.1467
REMARK 3 S31: 0.5206 S32: 0.2021 S33: 0.3782
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 14 J 106
REMARK 3 ORIGIN FOR THE GROUP (A): 69.8508 47.1506 13.8207
REMARK 3 T TENSOR
REMARK 3 T11: 1.3888 T22: 0.7718
REMARK 3 T33: 1.1224 T12: -0.0949
REMARK 3 T13: -0.1916 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 2.0970 L22: 0.3962
REMARK 3 L33: 6.3196 L12: -0.7560
REMARK 3 L13: -2.9861 L23: 1.4335
REMARK 3 S TENSOR
REMARK 3 S11: 0.3379 S12: 0.0782 S13: 0.1244
REMARK 3 S21: -0.2917 S22: -0.0474 S23: 0.1752
REMARK 3 S31: -0.5200 S32: 0.0047 S33: -0.2904
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 14 K 118
REMARK 3 ORIGIN FOR THE GROUP (A): 99.6577 15.0518 31.7910
REMARK 3 T TENSOR
REMARK 3 T11: 2.2075 T22: 2.0762
REMARK 3 T33: 2.0521 T12: -0.4260
REMARK 3 T13: -0.5760 T23: -0.2584
REMARK 3 L TENSOR
REMARK 3 L11: 1.9075 L22: 0.2198
REMARK 3 L33: 2.7033 L12: -0.6459
REMARK 3 L13: -2.1683 L23: 0.7241
REMARK 3 S TENSOR
REMARK 3 S11: 0.4188 S12: -0.3963 S13: 0.6731
REMARK 3 S21: -0.1194 S22: 0.0742 S23: -0.2172
REMARK 3 S31: -1.2081 S32: 0.3970 S33: -0.4930
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 8 L 81
REMARK 3 ORIGIN FOR THE GROUP (A): 93.7519 11.8089 31.4662
REMARK 3 T TENSOR
REMARK 3 T11: 1.1201 T22: 2.0961
REMARK 3 T33: 1.6511 T12: -0.0748
REMARK 3 T13: -0.1613 T23: -0.1226
REMARK 3 L TENSOR
REMARK 3 L11: 11.4125 L22: 2.4129
REMARK 3 L33: 0.3560 L12: 3.3425
REMARK 3 L13: 0.4495 L23: -0.4156
REMARK 3 S TENSOR
REMARK 3 S11: -1.1850 S12: 2.0499 S13: 0.4021
REMARK 3 S21: -0.3921 S22: 1.0446 S23: 0.9022
REMARK 3 S31: -0.1230 S32: -0.2535 S33: 0.1404
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 8 M 81
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6278 54.8707 40.2880
REMARK 3 T TENSOR
REMARK 3 T11: 1.3888 T22: 1.3291
REMARK 3 T33: 0.8799 T12: -0.1480
REMARK 3 T13: -0.0737 T23: -0.1327
REMARK 3 L TENSOR
REMARK 3 L11: 2.6002 L22: 0.2710
REMARK 3 L33: 1.8099 L12: 0.2671
REMARK 3 L13: -1.0044 L23: 0.4305
REMARK 3 S TENSOR
REMARK 3 S11: -0.1189 S12: -0.4590 S13: -0.1444
REMARK 3 S21: -0.2563 S22: -0.0162 S23: 0.2090
REMARK 3 S31: -0.5094 S32: 0.7143 S33: 0.1350
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 8 N 81
REMARK 3 ORIGIN FOR THE GROUP (A): 65.5000 48.8401 14.7165
REMARK 3 T TENSOR
REMARK 3 T11: 1.5022 T22: 1.8227
REMARK 3 T33: 0.3818 T12: 0.2950
REMARK 3 T13: 0.0638 T23: 0.3535
REMARK 3 L TENSOR
REMARK 3 L11: 5.1512 L22: 10.5489
REMARK 3 L33: 3.8895 L12: 2.1471
REMARK 3 L13: -1.9088 L23: 4.7290
REMARK 3 S TENSOR
REMARK 3 S11: 0.5366 S12: -0.0060 S13: -0.7848
REMARK 3 S21: -0.1995 S22: -1.3716 S23: 0.6713
REMARK 3 S31: -0.6175 S32: -0.7500 S33: 0.8351
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 14 Q 118
REMARK 3 ORIGIN FOR THE GROUP (A): 82.0489 -51.8456 19.5499
REMARK 3 T TENSOR
REMARK 3 T11: 1.4741 T22: 1.6231
REMARK 3 T33: 0.5811 T12: 0.0384
REMARK 3 T13: 0.0550 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 1.9280 L22: 0.8099
REMARK 3 L33: 0.1960 L12: -0.6837
REMARK 3 L13: 0.1054 L23: 0.1510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: 0.9988 S13: 0.6514
REMARK 3 S21: 0.2181 S22: 0.0747 S23: -0.0231
REMARK 3 S31: 0.3739 S32: 0.3881 S33: -0.0608
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 14 R 106
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1062 -46.5236 45.8118
REMARK 3 T TENSOR
REMARK 3 T11: 1.4102 T22: 1.4005
REMARK 3 T33: 1.4310 T12: -0.0707
REMARK 3 T13: -0.1395 T23: 0.2197
REMARK 3 L TENSOR
REMARK 3 L11: 1.6319 L22: 1.2465
REMARK 3 L33: 5.7709 L12: -1.3385
REMARK 3 L13: -2.1649 L23: 2.3039
REMARK 3 S TENSOR
REMARK 3 S11: 0.4233 S12: 0.2050 S13: -0.7592
REMARK 3 S21: 0.0165 S22: 0.0352 S23: 0.4493
REMARK 3 S31: 0.0259 S32: 0.0415 S33: -0.4585
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 14 S 106
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5600 -83.8431 1.5244
REMARK 3 T TENSOR
REMARK 3 T11: 1.1317 T22: 1.3393
REMARK 3 T33: 0.7867 T12: -0.0298
REMARK 3 T13: 0.5110 T23: 0.1101
REMARK 3 L TENSOR
REMARK 3 L11: 5.0406 L22: 3.7293
REMARK 3 L33: 2.8838 L12: -2.9591
REMARK 3 L13: 2.4362 L23: -0.3934
REMARK 3 S TENSOR
REMARK 3 S11: -0.3267 S12: 0.7236 S13: 0.7325
REMARK 3 S21: 0.1441 S22: 0.0107 S23: -0.1090
REMARK 3 S31: 0.2526 S32: 0.1054 S33: 0.3161
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 14 T 118
REMARK 3 ORIGIN FOR THE GROUP (A): 101.9905 -17.9497 30.8873
REMARK 3 T TENSOR
REMARK 3 T11: 2.0136 T22: 1.8956
REMARK 3 T33: 1.3851 T12: 0.0138
REMARK 3 T13: 0.3024 T23: -0.1038
REMARK 3 L TENSOR
REMARK 3 L11: 9.1666 L22: 1.5566
REMARK 3 L33: 3.2608 L12: -1.3716
REMARK 3 L13: 2.8517 L23: -1.5728
REMARK 3 S TENSOR
REMARK 3 S11: -0.5154 S12: 0.1203 S13: 0.3649
REMARK 3 S21: 0.1321 S22: 0.6109 S23: 0.0063
REMARK 3 S31: 1.3129 S32: -0.0332 S33: -0.0955
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 8 U 81
REMARK 3 ORIGIN FOR THE GROUP (A): 95.2643 -13.4009 31.9129
REMARK 3 T TENSOR
REMARK 3 T11: 1.6692 T22: 1.8241
REMARK 3 T33: 1.2627 T12: 0.1452
REMARK 3 T13: 0.3776 T23: -0.3976
REMARK 3 L TENSOR
REMARK 3 L11: 2.3415 L22: 1.1987
REMARK 3 L33: 2.9931 L12: -0.1347
REMARK 3 L13: 2.2464 L23: -1.1067
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: -1.3401 S13: 0.4468
REMARK 3 S21: 0.4570 S22: -0.2549 S23: 0.2085
REMARK 3 S31: -0.4114 S32: -0.8159 S33: 0.3781
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 8 V 81
REMARK 3 ORIGIN FOR THE GROUP (A): 74.4395 -54.5093 21.0426
REMARK 3 T TENSOR
REMARK 3 T11: 1.6205 T22: 1.2762
REMARK 3 T33: 0.6455 T12: 0.3396
REMARK 3 T13: 0.4457 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.0492 L22: 2.1954
REMARK 3 L33: 2.4200 L12: 2.8514
REMARK 3 L13: 1.2273 L23: -0.4037
REMARK 3 S TENSOR
REMARK 3 S11: 0.6276 S12: 0.8775 S13: 0.2828
REMARK 3 S21: 0.3660 S22: 0.3344 S23: 0.6687
REMARK 3 S31: -0.0621 S32: 0.2804 S33: -0.9620
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 8 W 81
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6569 -48.5601 44.5959
REMARK 3 T TENSOR
REMARK 3 T11: 1.2374 T22: 1.3546
REMARK 3 T33: 0.4447 T12: -0.1234
REMARK 3 T13: 0.1718 T23: 0.4002
REMARK 3 L TENSOR
REMARK 3 L11: 11.1202 L22: 6.5584
REMARK 3 L33: 7.4962 L12: 0.3376
REMARK 3 L13: 6.3816 L23: 3.2670
REMARK 3 S TENSOR
REMARK 3 S11: -0.3014 S12: 1.6163 S13: 2.0565
REMARK 3 S21: 0.1156 S22: -0.9903 S23: 0.2168
REMARK 3 S31: 0.5953 S32: -0.2336 S33: 1.2916
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 8 X 81
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9103 -80.6931 1.1298
REMARK 3 T TENSOR
REMARK 3 T11: 1.2516 T22: 1.8217
REMARK 3 T33: 1.0715 T12: 0.3569
REMARK 3 T13: 0.4795 T23: 0.3208
REMARK 3 L TENSOR
REMARK 3 L11: 2.9086 L22: 4.2795
REMARK 3 L33: 1.0052 L12: 3.5221
REMARK 3 L13: 1.6047 L23: 1.9823
REMARK 3 S TENSOR
REMARK 3 S11: -0.3635 S12: -0.2594 S13: 0.4075
REMARK 3 S21: -0.4147 S22: -0.1983 S23: 0.6110
REMARK 3 S31: 0.0968 S32: 0.0820 S33: 0.5618
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 14 Y 106
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4624 -33.7432 53.6999
REMARK 3 T TENSOR
REMARK 3 T11: 3.3779 T22: 3.4298
REMARK 3 T33: 2.0672 T12: 0.4009
REMARK 3 T13: -0.3716 T23: 0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 3.0724 L22: 4.1142
REMARK 3 L33: 0.7656 L12: 3.3835
REMARK 3 L13: -1.5079 L23: -1.7023
REMARK 3 S TENSOR
REMARK 3 S11: 1.1731 S12: -0.2331 S13: 0.9594
REMARK 3 S21: 0.7659 S22: -0.8923 S23: 0.5666
REMARK 3 S31: -0.7199 S32: 0.2751 S33: -0.2807
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 8 Z 81
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7077 -37.9618 52.5108
REMARK 3 T TENSOR
REMARK 3 T11: 1.4833 T22: 1.7724
REMARK 3 T33: 1.9608 T12: 0.1138
REMARK 3 T13: -0.1318 T23: 0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 0.5916 L22: 17.6570
REMARK 3 L33: 0.6260 L12: 3.1952
REMARK 3 L13: -0.4441 L23: -2.6999
REMARK 3 S TENSOR
REMARK 3 S11: 0.1296 S12: 0.0101 S13: -0.1474
REMARK 3 S21: 0.7457 S22: -0.7570 S23: -1.0620
REMARK 3 S31: -0.2344 S32: 0.5018 S33: 0.6273
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 14 a 106
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7325 -54.6458 58.7554
REMARK 3 T TENSOR
REMARK 3 T11: 1.8483 T22: 2.2146
REMARK 3 T33: 2.4251 T12: 0.1004
REMARK 3 T13: 0.1576 T23: -0.2039
REMARK 3 L TENSOR
REMARK 3 L11: 1.1994 L22: 4.8000
REMARK 3 L33: 6.5248 L12: 2.2078
REMARK 3 L13: 0.7226 L23: 3.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: 0.1762 S13: -0.1677
REMARK 3 S21: 0.5407 S22: -0.6455 S23: 0.0523
REMARK 3 S31: -0.0956 S32: -0.7919 S33: 0.6246
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 8 b 81
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9466 -58.2275 58.2215
REMARK 3 T TENSOR
REMARK 3 T11: 1.6781 T22: 1.3037
REMARK 3 T33: 1.8553 T12: 0.3107
REMARK 3 T13: 0.1436 T23: -0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 12.1326 L22: 7.1188
REMARK 3 L33: 7.7539 L12: -0.0990
REMARK 3 L13: 2.3417 L23: 7.1595
REMARK 3 S TENSOR
REMARK 3 S11: -0.2391 S12: 0.4230 S13: -2.0513
REMARK 3 S21: 0.7626 S22: -0.4389 S23: 0.9175
REMARK 3 S31: 0.4938 S32: -0.5352 S33: 0.6780
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : c 14 c 106
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4183 -96.6002 59.8054
REMARK 3 T TENSOR
REMARK 3 T11: 1.0436 T22: 1.1996
REMARK 3 T33: 1.3899 T12: -0.2306
REMARK 3 T13: 0.5317 T23: 0.5007
REMARK 3 L TENSOR
REMARK 3 L11: 2.3107 L22: 10.0851
REMARK 3 L33: 9.4556 L12: -2.9072
REMARK 3 L13: -0.5898 L23: 8.4424
REMARK 3 S TENSOR
REMARK 3 S11: 0.4505 S12: 0.4962 S13: 0.9868
REMARK 3 S21: 0.5279 S22: -0.3978 S23: -0.8560
REMARK 3 S31: 1.1011 S32: 0.1515 S33: -0.0526
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : d 8 d 81
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8141 -92.2656 61.0597
REMARK 3 T TENSOR
REMARK 3 T11: 1.2436 T22: 1.5766
REMARK 3 T33: 1.7865 T12: -0.0778
REMARK 3 T13: -0.0119 T23: -0.0880
REMARK 3 L TENSOR
REMARK 3 L11: 2.3646 L22: 9.1603
REMARK 3 L33: 14.4547 L12: -1.9433
REMARK 3 L13: -4.7919 L23: 8.6670
REMARK 3 S TENSOR
REMARK 3 S11: 0.4064 S12: -0.1333 S13: 0.4928
REMARK 3 S21: -0.0412 S22: -1.3688 S23: 1.1247
REMARK 3 S31: 0.3694 S32: -0.5038 S33: 0.9624
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : e 14 e 118
REMARK 3 ORIGIN FOR THE GROUP (A): 81.6865 51.7437 106.8941
REMARK 3 T TENSOR
REMARK 3 T11: 1.8839 T22: 1.8418
REMARK 3 T33: 0.9916 T12: -0.0194
REMARK 3 T13: -0.2699 T23: -0.2200
REMARK 3 L TENSOR
REMARK 3 L11: 3.1755 L22: 5.4995
REMARK 3 L33: 2.1626 L12: 2.3522
REMARK 3 L13: -1.7069 L23: -3.4112
REMARK 3 S TENSOR
REMARK 3 S11: -0.7153 S12: -0.6946 S13: 0.0189
REMARK 3 S21: -0.6515 S22: 0.0058 S23: -1.2578
REMARK 3 S31: 0.4636 S32: 0.2503 S33: 0.7095
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : f 14 f 106
REMARK 3 ORIGIN FOR THE GROUP (A): 70.7565 47.3506 78.8231
REMARK 3 T TENSOR
REMARK 3 T11: 1.4745 T22: 1.4904
REMARK 3 T33: 1.6048 T12: 0.0607
REMARK 3 T13: 0.1058 T23: 0.3688
REMARK 3 L TENSOR
REMARK 3 L11: 0.4225 L22: 2.7068
REMARK 3 L33: 3.6391 L12: -0.2155
REMARK 3 L13: 0.4120 L23: 2.5617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0986 S12: -0.1031 S13: -0.2125
REMARK 3 S21: -0.1528 S22: 0.3397 S23: 0.3039
REMARK 3 S31: 0.1373 S32: -0.2805 S33: -0.4383
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : g 14 g 118
REMARK 3 ORIGIN FOR THE GROUP (A): 99.5784 14.9797 97.4105
REMARK 3 T TENSOR
REMARK 3 T11: 2.7714 T22: 2.7242
REMARK 3 T33: 2.3635 T12: -0.2426
REMARK 3 T13: -0.8271 T23: -0.1139
REMARK 3 L TENSOR
REMARK 3 L11: 1.2525 L22: 0.3955
REMARK 3 L33: 3.1445 L12: -0.1939
REMARK 3 L13: -1.2649 L23: 0.7364
REMARK 3 S TENSOR
REMARK 3 S11: -0.6819 S12: -0.4812 S13: 0.8316
REMARK 3 S21: -0.6075 S22: 0.7096 S23: 0.3358
REMARK 3 S31: -1.1772 S32: 0.1976 S33: -0.0277
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : h 8 h 81
REMARK 3 ORIGIN FOR THE GROUP (A): 93.8040 11.3479 96.9090
REMARK 3 T TENSOR
REMARK 3 T11: 2.0758 T22: 2.1966
REMARK 3 T33: 2.6104 T12: 0.0025
REMARK 3 T13: -0.6281 T23: -0.2561
REMARK 3 L TENSOR
REMARK 3 L11: 2.0020 L22: 0.4213
REMARK 3 L33: 2.7339 L12: 0.8367
REMARK 3 L13: -2.1853 L23: -0.8127
REMARK 3 S TENSOR
REMARK 3 S11: -0.8914 S12: 1.2072 S13: -0.3136
REMARK 3 S21: -0.5506 S22: 0.1741 S23: 0.1882
REMARK 3 S31: 0.0828 S32: -1.3936 S33: 0.7173
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : i 8 i 81
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1209 54.7477 106.4995
REMARK 3 T TENSOR
REMARK 3 T11: 1.7678 T22: 2.0521
REMARK 3 T33: 1.2096 T12: -0.1180
REMARK 3 T13: -0.1259 T23: -0.2045
REMARK 3 L TENSOR
REMARK 3 L11: 2.1343 L22: 0.0918
REMARK 3 L33: 4.1800 L12: 0.2721
REMARK 3 L13: 0.4158 L23: 0.2813
REMARK 3 S TENSOR
REMARK 3 S11: 0.6471 S12: 0.4136 S13: 0.8032
REMARK 3 S21: 0.0198 S22: -0.2740 S23: 0.1357
REMARK 3 S31: 0.1506 S32: 0.6971 S33: -0.3732
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : j 8 j 81
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9494 49.3266 79.5394
REMARK 3 T TENSOR
REMARK 3 T11: 1.8680 T22: 2.1513
REMARK 3 T33: 1.6732 T12: 0.3065
REMARK 3 T13: 0.3083 T23: 0.0950
REMARK 3 L TENSOR
REMARK 3 L11: 5.6057 L22: 3.9572
REMARK 3 L33: 4.8408 L12: 4.4982
REMARK 3 L13: -5.0467 L23: -3.8292
REMARK 3 S TENSOR
REMARK 3 S11: -0.3296 S12: -0.3407 S13: -0.3691
REMARK 3 S21: 0.1453 S22: -0.0486 S23: -0.1447
REMARK 3 S31: 0.3550 S32: -0.0554 S33: 0.3782
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : k 14 k 118
REMARK 3 ORIGIN FOR THE GROUP (A): 81.5526 -52.1916 85.5817
REMARK 3 T TENSOR
REMARK 3 T11: 1.3359 T22: 1.4751
REMARK 3 T33: 1.0694 T12: 0.0096
REMARK 3 T13: 0.0593 T23: -0.2064
REMARK 3 L TENSOR
REMARK 3 L11: 7.0467 L22: 5.6207
REMARK 3 L33: 2.9205 L12: 4.1683
REMARK 3 L13: -1.1857 L23: -3.4143
REMARK 3 S TENSOR
REMARK 3 S11: -0.4100 S12: 0.1713 S13: -0.7683
REMARK 3 S21: 0.0020 S22: -0.1354 S23: -0.3465
REMARK 3 S31: -0.5659 S32: 0.2247 S33: 0.5453
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : l 14 l 106
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1199 -46.5721 111.0234
REMARK 3 T TENSOR
REMARK 3 T11: 1.6333 T22: 1.5420
REMARK 3 T33: 1.4225 T12: -0.0238
REMARK 3 T13: -0.0469 T23: 0.2579
REMARK 3 L TENSOR
REMARK 3 L11: 5.8513 L22: 8.1695
REMARK 3 L33: 4.8199 L12: 3.6052
REMARK 3 L13: 0.8696 L23: -0.4173
REMARK 3 S TENSOR
REMARK 3 S11: 0.8513 S12: 0.1011 S13: -0.8736
REMARK 3 S21: 0.3645 S22: -0.8279 S23: -0.1092
REMARK 3 S31: 0.0572 S32: -0.2723 S33: -0.0234
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : m 14 m 106
REMARK 3 ORIGIN FOR THE GROUP (A): 62.7701 -83.8451 67.8306
REMARK 3 T TENSOR
REMARK 3 T11: 1.1235 T22: 1.7073
REMARK 3 T33: 1.9531 T12: -0.1031
REMARK 3 T13: 0.4528 T23: 0.1317
REMARK 3 L TENSOR
REMARK 3 L11: 2.7445 L22: 12.8264
REMARK 3 L33: 8.4850 L12: -5.3931
REMARK 3 L13: 1.3875 L23: 0.9849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0782 S12: 0.1457 S13: -0.5929
REMARK 3 S21: 0.4404 S22: 0.3891 S23: 1.6709
REMARK 3 S31: 0.8838 S32: -0.0061 S33: -0.3109
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : n 14 n 118
REMARK 3 ORIGIN FOR THE GROUP (A): 101.9427 -17.6462 95.7333
REMARK 3 T TENSOR
REMARK 3 T11: 2.0758 T22: 2.3154
REMARK 3 T33: 1.7774 T12: 0.0261
REMARK 3 T13: 0.2726 T23: -0.1434
REMARK 3 L TENSOR
REMARK 3 L11: 8.5968 L22: 0.4457
REMARK 3 L33: 2.8715 L12: 1.0210
REMARK 3 L13: 3.4656 L23: -0.1715
REMARK 3 S TENSOR
REMARK 3 S11: -0.7436 S12: 0.7174 S13: 0.2804
REMARK 3 S21: -0.3986 S22: 0.1997 S23: -0.1696
REMARK 3 S31: 1.0962 S32: -0.0236 S33: 0.5439
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : o 8 o 81
REMARK 3 ORIGIN FOR THE GROUP (A): 94.9744 -13.4902 95.7425
REMARK 3 T TENSOR
REMARK 3 T11: 1.8700 T22: 2.0449
REMARK 3 T33: 1.7034 T12: 0.0627
REMARK 3 T13: -0.1023 T23: -0.2262
REMARK 3 L TENSOR
REMARK 3 L11: 4.2874 L22: 5.5477
REMARK 3 L33: 6.2495 L12: 4.3118
REMARK 3 L13: -3.3155 L23: -4.9970
REMARK 3 S TENSOR
REMARK 3 S11: -0.3154 S12: -0.7487 S13: 0.0903
REMARK 3 S21: 0.1902 S22: -0.4195 S23: 0.1841
REMARK 3 S31: 0.5901 S32: -0.5815 S33: 0.7349
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : p 8 p 81
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1232 -54.3575 86.5850
REMARK 3 T TENSOR
REMARK 3 T11: 1.9866 T22: 2.0097
REMARK 3 T33: 0.4619 T12: 0.2357
REMARK 3 T13: 0.1314 T23: -0.2342
REMARK 3 L TENSOR
REMARK 3 L11: 10.8541 L22: 7.8797
REMARK 3 L33: 4.0054 L12: 7.2317
REMARK 3 L13: -3.5417 L23: -4.1959
REMARK 3 S TENSOR
REMARK 3 S11: -0.2750 S12: 0.6283 S13: -1.2547
REMARK 3 S21: 1.2629 S22: -0.1122 S23: -0.7898
REMARK 3 S31: -0.2536 S32: -0.4511 S33: 0.3872
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : q 8 q 81
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2811 -48.4382 109.7206
REMARK 3 T TENSOR
REMARK 3 T11: 1.6113 T22: 1.7398
REMARK 3 T33: 1.6768 T12: -0.0998
REMARK 3 T13: 0.4095 T23: 0.2102
REMARK 3 L TENSOR
REMARK 3 L11: 9.5535 L22: 4.1183
REMARK 3 L33: 10.7265 L12: 2.3423
REMARK 3 L13: 9.3677 L23: 4.4647
REMARK 3 S TENSOR
REMARK 3 S11: -1.2649 S12: -0.4579 S13: 0.7248
REMARK 3 S21: 0.4793 S22: -0.0608 S23: 0.3478
REMARK 3 S31: -0.5507 S32: -0.6791 S33: 1.3257
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : r 8 r 81
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0110 -80.1868 67.5929
REMARK 3 T TENSOR
REMARK 3 T11: 1.3977 T22: 1.5588
REMARK 3 T33: 2.2995 T12: -0.0492
REMARK 3 T13: -0.1238 T23: 0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 3.7759 L22: 0.7246
REMARK 3 L33: 8.5879 L12: 1.5521
REMARK 3 L13: -5.5183 L23: -2.1484
REMARK 3 S TENSOR
REMARK 3 S11: -0.8030 S12: -0.2116 S13: -0.3198
REMARK 3 S21: -0.1508 S22: -0.2238 S23: 0.0829
REMARK 3 S31: 0.9638 S32: 0.9224 S33: 1.0268
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 26
REMARK 3 ORIGIN FOR THE GROUP (A): 116.4799 28.2422 45.8036
REMARK 3 T TENSOR
REMARK 3 T11: 1.5003 T22: 1.4622
REMARK 3 T33: 1.4224 T12: -0.1543
REMARK 3 T13: 0.1178 T23: -0.2033
REMARK 3 L TENSOR
REMARK 3 L11: 0.0675 L22: 0.2085
REMARK 3 L33: 0.7137 L12: -0.1019
REMARK 3 L13: 0.0963 L23: -0.2627
REMARK 3 S TENSOR
REMARK 3 S11: -0.2904 S12: 0.1007 S13: 0.0705
REMARK 3 S21: 0.2481 S22: -0.1296 S23: -0.3661
REMARK 3 S31: 0.2110 S32: -0.0501 S33: 0.4200
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 26
REMARK 3 ORIGIN FOR THE GROUP (A): 116.4296 27.2427 45.0467
REMARK 3 T TENSOR
REMARK 3 T11: 1.3733 T22: 1.1090
REMARK 3 T33: 1.2084 T12: -0.2861
REMARK 3 T13: -0.1518 T23: 0.1201
REMARK 3 L TENSOR
REMARK 3 L11: 7.3784 L22: 1.7889
REMARK 3 L33: 3.8631 L12: -0.9300
REMARK 3 L13: -3.8122 L23: 0.7849
REMARK 3 S TENSOR
REMARK 3 S11: -1.5635 S12: 1.3597 S13: 1.4399
REMARK 3 S21: 0.2655 S22: 1.0522 S23: -0.4120
REMARK 3 S31: 0.8791 S32: -0.4483 S33: 0.5113
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 26
REMARK 3 ORIGIN FOR THE GROUP (A): 113.7269 -29.6076 81.3191
REMARK 3 T TENSOR
REMARK 3 T11: 4.0253 T22: 3.4053
REMARK 3 T33: 0.9298 T12: 1.1777
REMARK 3 T13: 0.5373 T23: 0.7285
REMARK 3 L TENSOR
REMARK 3 L11: 22.9895 L22: 12.6030
REMARK 3 L33: 4.8241 L12: 14.3548
REMARK 3 L13: 0.4896 L23: 3.3134
REMARK 3 S TENSOR
REMARK 3 S11: 1.2107 S12: 3.1173 S13: 0.1532
REMARK 3 S21: 1.3108 S22: -0.1074 S23: -1.3168
REMARK 3 S31: 1.7180 S32: 0.2529 S33: -1.1033
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 26
REMARK 3 ORIGIN FOR THE GROUP (A): 113.9190 -28.2930 81.7598
REMARK 3 T TENSOR
REMARK 3 T11: 1.7815 T22: 1.5223
REMARK 3 T33: 1.2988 T12: 0.0792
REMARK 3 T13: -0.0139 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 10.8031 L22: 3.2692
REMARK 3 L33: 2.7321 L12: 4.5477
REMARK 3 L13: 3.3390 L23: 1.1826
REMARK 3 S TENSOR
REMARK 3 S11: -1.8786 S12: -1.2508 S13: -0.6450
REMARK 3 S21: -0.8370 S22: 0.7451 S23: -0.5611
REMARK 3 S31: -1.3954 S32: -0.2089 S33: 1.1335
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : s 1 s 26
REMARK 3 ORIGIN FOR THE GROUP (A): 114.5846 -29.2096 15.6262
REMARK 3 T TENSOR
REMARK 3 T11: 4.1166 T22: 3.9630
REMARK 3 T33: 2.3174 T12: 0.4261
REMARK 3 T13: 0.7917 T23: -0.2118
REMARK 3 L TENSOR
REMARK 3 L11: 3.6526 L22: 0.7276
REMARK 3 L33: 3.6642 L12: 1.4053
REMARK 3 L13: 0.5443 L23: -0.4721
REMARK 3 S TENSOR
REMARK 3 S11: -0.2620 S12: 0.6782 S13: 0.4935
REMARK 3 S21: -0.2149 S22: -0.0668 S23: -0.1648
REMARK 3 S31: 0.1379 S32: 0.7460 S33: 0.3288
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : t 1 t 26
REMARK 3 ORIGIN FOR THE GROUP (A): 114.2340 -28.1407 15.8692
REMARK 3 T TENSOR
REMARK 3 T11: 1.8428 T22: 1.6410
REMARK 3 T33: 1.4105 T12: 0.1707
REMARK 3 T13: -0.0074 T23: 0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 11.9255 L22: 2.7865
REMARK 3 L33: 5.4489 L12: 4.3141
REMARK 3 L13: 5.2117 L23: 1.7514
REMARK 3 S TENSOR
REMARK 3 S11: -2.1065 S12: -1.4787 S13: -0.7039
REMARK 3 S21: -0.9850 S22: 0.6487 S23: -0.3625
REMARK 3 S31: -1.6583 S32: -0.2472 S33: 1.4578
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : u 1 u 26
REMARK 3 ORIGIN FOR THE GROUP (A): 115.5440 28.7744 112.0296
REMARK 3 T TENSOR
REMARK 3 T11: 1.7987 T22: 1.7197
REMARK 3 T33: 1.9022 T12: -0.2481
REMARK 3 T13: -0.1158 T23: 0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 0.2505 L22: 0.5794
REMARK 3 L33: 0.7324 L12: 0.0554
REMARK 3 L13: 0.1053 L23: -0.3073
REMARK 3 S TENSOR
REMARK 3 S11: -0.4527 S12: 0.3757 S13: 0.3368
REMARK 3 S21: 0.3042 S22: 0.0958 S23: -0.2025
REMARK 3 S31: 0.1869 S32: -0.0230 S33: 0.3569
REMARK 3
REMARK 3 TLS GROUP : 48
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : v 1 v 26
REMARK 3 ORIGIN FOR THE GROUP (A): 116.0535 27.1671 111.1339
REMARK 3 T TENSOR
REMARK 3 T11: 1.5952 T22: 1.4291
REMARK 3 T33: 1.4511 T12: -0.2324
REMARK 3 T13: -0.2228 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 15.2380 L22: 3.3888
REMARK 3 L33: 4.1284 L12: -4.1385
REMARK 3 L13: -5.1275 L23: 1.7074
REMARK 3 S TENSOR
REMARK 3 S11: -2.1401 S12: 0.8796 S13: 2.5284
REMARK 3 S21: 0.8667 S22: 1.4932 S23: -0.9483
REMARK 3 S31: 1.3157 S32: -0.1107 S33: 0.6469
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.30
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4NE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083084.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18329
REMARK 200 RESOLUTION RANGE HIGH (A) : 6.499
REMARK 200 RESOLUTION RANGE LOW (A) : 112.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.3M AMMONIUM PHOSPHATE, MICRO
REMARK 280 -BATCH UNDER OIL, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, s, t, C, D, G, H, A, B,
REMARK 350 AND CHAINS: I, J, K, L, M, N, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P, u, v, Y, Z, a, b, c, d,
REMARK 350 AND CHAINS: e, f, g, h, i, j, k, l, m,
REMARK 350 AND CHAINS: n, o, p, q, r
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN C 107
REMARK 465 LEU C 108
REMARK 465 GLU C 109
REMARK 465 ARG C 110
REMARK 465 LYS C 111
REMARK 465 ALA C 112
REMARK 465 GLN C 113
REMARK 465 LYS C 114
REMARK 465 LYS C 115
REMARK 465 LYS C 116
REMARK 465 LYS C 117
REMARK 465 SER C 118
REMARK 465 ASN G 107
REMARK 465 LEU G 108
REMARK 465 GLU G 109
REMARK 465 ARG G 110
REMARK 465 LYS G 111
REMARK 465 ALA G 112
REMARK 465 GLN G 113
REMARK 465 LYS G 114
REMARK 465 LYS G 115
REMARK 465 LYS G 116
REMARK 465 LYS G 117
REMARK 465 SER G 118
REMARK 465 ASN A 107
REMARK 465 LEU A 108
REMARK 465 GLU A 109
REMARK 465 ARG A 110
REMARK 465 LYS A 111
REMARK 465 ALA A 112
REMARK 465 GLN A 113
REMARK 465 LYS A 114
REMARK 465 LYS A 115
REMARK 465 LYS A 116
REMARK 465 LYS A 117
REMARK 465 SER A 118
REMARK 465 ASN J 107
REMARK 465 LEU J 108
REMARK 465 GLU J 109
REMARK 465 ARG J 110
REMARK 465 LYS J 111
REMARK 465 ALA J 112
REMARK 465 GLN J 113
REMARK 465 LYS J 114
REMARK 465 LYS J 115
REMARK 465 LYS J 116
REMARK 465 LYS J 117
REMARK 465 SER J 118
REMARK 465 ASN R 107
REMARK 465 LEU R 108
REMARK 465 GLU R 109
REMARK 465 ARG R 110
REMARK 465 LYS R 111
REMARK 465 ALA R 112
REMARK 465 GLN R 113
REMARK 465 LYS R 114
REMARK 465 LYS R 115
REMARK 465 LYS R 116
REMARK 465 LYS R 117
REMARK 465 SER R 118
REMARK 465 ASN S 107
REMARK 465 LEU S 108
REMARK 465 GLU S 109
REMARK 465 ARG S 110
REMARK 465 LYS S 111
REMARK 465 ALA S 112
REMARK 465 GLN S 113
REMARK 465 LYS S 114
REMARK 465 LYS S 115
REMARK 465 LYS S 116
REMARK 465 LYS S 117
REMARK 465 SER S 118
REMARK 465 ASN Y 107
REMARK 465 LEU Y 108
REMARK 465 GLU Y 109
REMARK 465 ARG Y 110
REMARK 465 LYS Y 111
REMARK 465 ALA Y 112
REMARK 465 GLN Y 113
REMARK 465 LYS Y 114
REMARK 465 LYS Y 115
REMARK 465 LYS Y 116
REMARK 465 LYS Y 117
REMARK 465 SER Y 118
REMARK 465 ASN a 107
REMARK 465 LEU a 108
REMARK 465 GLU a 109
REMARK 465 ARG a 110
REMARK 465 LYS a 111
REMARK 465 ALA a 112
REMARK 465 GLN a 113
REMARK 465 LYS a 114
REMARK 465 LYS a 115
REMARK 465 LYS a 116
REMARK 465 LYS a 117
REMARK 465 SER a 118
REMARK 465 ASN c 107
REMARK 465 LEU c 108
REMARK 465 GLU c 109
REMARK 465 ARG c 110
REMARK 465 LYS c 111
REMARK 465 ALA c 112
REMARK 465 GLN c 113
REMARK 465 LYS c 114
REMARK 465 LYS c 115
REMARK 465 LYS c 116
REMARK 465 LYS c 117
REMARK 465 SER c 118
REMARK 465 ASN f 107
REMARK 465 LEU f 108
REMARK 465 GLU f 109
REMARK 465 ARG f 110
REMARK 465 LYS f 111
REMARK 465 ALA f 112
REMARK 465 GLN f 113
REMARK 465 LYS f 114
REMARK 465 LYS f 115
REMARK 465 LYS f 116
REMARK 465 LYS f 117
REMARK 465 SER f 118
REMARK 465 ASN l 107
REMARK 465 LEU l 108
REMARK 465 GLU l 109
REMARK 465 ARG l 110
REMARK 465 LYS l 111
REMARK 465 ALA l 112
REMARK 465 GLN l 113
REMARK 465 LYS l 114
REMARK 465 LYS l 115
REMARK 465 LYS l 116
REMARK 465 LYS l 117
REMARK 465 SER l 118
REMARK 465 ASN m 107
REMARK 465 LEU m 108
REMARK 465 GLU m 109
REMARK 465 ARG m 110
REMARK 465 LYS m 111
REMARK 465 ALA m 112
REMARK 465 GLN m 113
REMARK 465 LYS m 114
REMARK 465 LYS m 115
REMARK 465 LYS m 116
REMARK 465 LYS m 117
REMARK 465 SER m 118
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 PHE r 81 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C2 DA E 25 O2 DT F 2 1.77
REMARK 500 C2 DA E 24 O2 DT F 3 1.91
REMARK 500 OP1 DT P 13 O VAL o 30 1.96
REMARK 500 C2 DA u 26 O2 DT v 1 1.97
REMARK 500 OG1 THR T 26 NH1 ARG U 11 1.99
REMARK 500 OP2 DT t 14 NH1 ARG U 17 2.00
REMARK 500 OG SER Y 43 O VAL Z 65 2.04
REMARK 500 N1 DA E 26 O2 DT F 1 2.10
REMARK 500 N6 DA E 11 O4 DT F 16 2.10
REMARK 500 N6 DA u 11 O4 DT v 16 2.14
REMARK 500 ND2 ASN n 107 OD2 ASP o 33 2.16
REMARK 500 OE2 GLU J 33 OG SER N 8 2.19
REMARK 500 O THR Y 75 N LYS Z 29 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O2 DT v 4 OH TYR A 15 3656 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS G 29 CA - CB - SG ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU G 36 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU H 79 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 LEU B 79 CA - CB - CG ANGL. DEV. = 16.7 DEGREES
REMARK 500 LEU Q 36 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU S 36 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU T 53 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU U 74 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA C 86 43.96 -102.75
REMARK 500 ASP D 61 62.46 31.43
REMARK 500 GLN D 69 -72.24 -67.63
REMARK 500 ASN G 78 -167.22 -114.66
REMARK 500 MET A 40 147.47 -174.44
REMARK 500 ALA A 86 34.22 -88.04
REMARK 500 ASP B 61 59.98 70.49
REMARK 500 TYR I 15 -37.66 -39.09
REMARK 500 ALA I 86 42.87 -93.09
REMARK 500 LYS I 117 -73.64 -31.32
REMARK 500 ALA J 86 53.92 -116.16
REMARK 500 ASN K 78 -165.79 -123.53
REMARK 500 ALA K 86 50.13 -105.46
REMARK 500 ASP L 61 69.10 38.00
REMARK 500 ASP N 61 77.01 70.40
REMARK 500 ALA R 86 38.91 -99.40
REMARK 500 ASP W 26 3.31 -68.30
REMARK 500 ALA f 86 30.81 -90.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU D 63 ARG D 64 139.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NDY RELATED DB: PDB
DBREF 4NE1 C 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 D 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 G 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 H 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 A 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 B 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 I 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 J 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 K 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 L 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 M 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 N 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 Q 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 R 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 S 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 T 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 U 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 V 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 W 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 X 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 Y 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 Z 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 a 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 b 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 c 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 d 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 e 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 f 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 g 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 h 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 i 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 j 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 k 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 l 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 m 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 n 14 118 UNP Q8N2Z9 CENPS_HUMAN 14 118
DBREF 4NE1 o 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 p 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 q 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 r 8 81 UNP A8MT69 CENPX_HUMAN 8 81
DBREF 4NE1 E 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 O 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 s 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 u 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 F 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 P 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 t 1 26 PDB 4NE1 4NE1 1 26
DBREF 4NE1 v 1 26 PDB 4NE1 4NE1 1 26
SEQADV 4NE1 ALA C 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA C 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA G 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA G 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA A 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA A 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA I 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA I 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA J 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA J 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA K 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA K 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA Q 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA Q 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA R 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA R 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA S 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA S 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA T 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA T 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA Y 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA Y 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA a 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA a 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA c 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA c 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA e 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA e 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA f 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA f 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA g 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA g 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA k 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA k 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA l 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA l 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA m 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA m 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQADV 4NE1 ALA n 39 UNP Q8N2Z9 GLU 39 CONFLICT
SEQADV 4NE1 ALA n 106 UNP Q8N2Z9 ILE 106 CONFLICT
SEQRES 1 E 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 E 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 F 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 F 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 O 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 O 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 P 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 P 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 s 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 s 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 t 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 t 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 u 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 2 u 26 DA DA DA DA DA DA DA DA DA DA DA DA DA
SEQRES 1 v 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 v 26 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 1 C 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 C 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 C 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 C 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 C 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 C 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 C 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 C 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 C 105 SER
SEQRES 1 D 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 D 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 D 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 D 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 D 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 D 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 G 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 G 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 G 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 G 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 G 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 G 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 G 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 G 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 G 105 SER
SEQRES 1 H 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 H 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 H 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 H 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 H 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 H 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 A 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 A 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 A 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 A 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 A 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 A 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 A 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 A 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 A 105 SER
SEQRES 1 B 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 B 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 B 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 B 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 B 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 B 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 I 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 I 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 I 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 I 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 I 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 I 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 I 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 I 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 I 105 SER
SEQRES 1 J 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 J 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 J 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 J 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 J 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 J 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 J 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 J 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 J 105 SER
SEQRES 1 K 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 K 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 K 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 K 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 K 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 K 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 K 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 K 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 K 105 SER
SEQRES 1 L 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 L 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 L 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 L 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 L 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 L 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 M 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 M 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 M 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 M 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 M 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 M 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 N 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 N 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 N 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 N 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 N 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 N 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 Q 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 Q 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 Q 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 Q 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 Q 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 Q 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 Q 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 Q 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 Q 105 SER
SEQRES 1 R 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 R 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 R 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 R 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 R 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 R 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 R 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 R 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 R 105 SER
SEQRES 1 S 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 S 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 S 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 S 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 S 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 S 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 S 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 S 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 S 105 SER
SEQRES 1 T 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 T 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 T 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 T 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 T 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 T 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 T 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 T 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 T 105 SER
SEQRES 1 U 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 U 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 U 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 U 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 U 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 U 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 V 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 V 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 V 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 V 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 V 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 V 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 W 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 W 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 W 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 W 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 W 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 W 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 X 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 X 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 X 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 X 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 X 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 X 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 Y 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 Y 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 Y 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 Y 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 Y 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 Y 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 Y 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 Y 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 Y 105 SER
SEQRES 1 Z 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 Z 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 Z 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 Z 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 Z 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 Z 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 a 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 a 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 a 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 a 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 a 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 a 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 a 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 a 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 a 105 SER
SEQRES 1 b 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 b 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 b 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 b 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 b 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 b 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 c 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 c 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 c 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 c 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 c 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 c 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 c 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 c 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 c 105 SER
SEQRES 1 d 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 d 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 d 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 d 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 d 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 d 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 e 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 e 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 e 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 e 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 e 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 e 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 e 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 e 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 e 105 SER
SEQRES 1 f 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 f 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 f 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 f 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 f 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 f 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 f 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 f 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 f 105 SER
SEQRES 1 g 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 g 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 g 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 g 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 g 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 g 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 g 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 g 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 g 105 SER
SEQRES 1 h 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 h 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 h 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 h 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 h 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 h 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 i 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 i 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 i 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 i 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 i 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 i 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 j 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 j 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 j 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 j 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 j 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 j 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 k 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 k 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 k 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 k 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 k 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 k 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 k 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 k 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 k 105 SER
SEQRES 1 l 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 l 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 l 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 l 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 l 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 l 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 l 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 l 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 l 105 SER
SEQRES 1 m 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 m 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 m 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 m 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 m 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 m 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 m 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 m 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 m 105 SER
SEQRES 1 n 105 SER TYR GLN GLN ARG LEU LYS ALA ALA VAL HIS TYR THR
SEQRES 2 n 105 VAL GLY CYS LEU CYS GLU GLU VAL ALA LEU ASP LYS ALA
SEQRES 3 n 105 MET GLN PHE SER LYS GLN THR ILE ALA ALA ILE SER GLU
SEQRES 4 n 105 LEU THR PHE ARG GLN CYS GLU ASN PHE ALA LYS ASP LEU
SEQRES 5 n 105 GLU MET PHE ALA ARG HIS ALA LYS ARG THR THR ILE ASN
SEQRES 6 n 105 THR GLU ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER
SEQRES 7 n 105 LEU LEU LYS TYR ILE THR ASP LYS SER GLU GLU ILE ALA
SEQRES 8 n 105 GLN ALA ASN LEU GLU ARG LYS ALA GLN LYS LYS LYS LYS
SEQRES 9 n 105 SER
SEQRES 1 o 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 o 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 o 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 o 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 o 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 o 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 p 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 p 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 p 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 p 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 p 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 p 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 q 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 q 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 q 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 q 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 q 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 q 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
SEQRES 1 r 74 SER GLY PHE ARG LYS GLU LEU VAL SER ARG LEU LEU HIS
SEQRES 2 r 74 LEU HIS PHE LYS ASP ASP LYS THR LYS VAL SER GLY ASP
SEQRES 3 r 74 ALA LEU GLN LEU MET VAL GLU LEU LEU LYS VAL PHE VAL
SEQRES 4 r 74 VAL GLU ALA ALA VAL ARG GLY VAL ARG GLN ALA GLN ALA
SEQRES 5 r 74 GLU ASP ALA LEU ARG VAL ASP VAL ASP GLN LEU GLU LYS
SEQRES 6 r 74 VAL LEU PRO GLN LEU LEU LEU ASP PHE
HELIX 1 1 SER C 14 LYS C 38 1 25
HELIX 2 2 SER C 43 ALA C 72 1 30
HELIX 3 3 ASN C 78 LEU C 85 1 8
HELIX 4 4 SER C 89 ALA C 106 1 18
HELIX 5 5 ARG D 11 HIS D 22 1 12
HELIX 6 6 SER D 31 GLU D 60 1 30
HELIX 7 7 ASP D 66 PHE D 81 1 16
HELIX 8 8 TYR G 15 LYS G 38 1 24
HELIX 9 9 SER G 43 ALA G 72 1 30
HELIX 10 10 ASN G 78 ALA G 86 1 9
HELIX 11 11 SER G 89 GLN G 105 1 17
HELIX 12 12 ARG H 11 PHE H 23 1 13
HELIX 13 13 SER H 31 GLU H 60 1 30
HELIX 14 14 ASP H 66 VAL H 73 1 8
HELIX 15 15 VAL H 73 PHE H 81 1 9
HELIX 16 16 TYR A 15 LYS A 38 1 24
HELIX 17 17 SER A 43 ALA A 72 1 30
HELIX 18 18 ASN A 78 ALA A 86 1 9
HELIX 19 19 SER A 89 GLN A 105 1 17
HELIX 20 20 ARG B 11 LEU B 21 1 11
HELIX 21 21 SER B 31 GLU B 60 1 30
HELIX 22 22 ASP B 66 ASP B 80 1 15
HELIX 23 23 TYR I 15 ALA I 39 1 25
HELIX 24 24 SER I 43 ALA I 72 1 30
HELIX 25 25 ASN I 78 LEU I 84 1 7
HELIX 26 26 SER I 89 LYS I 114 1 26
HELIX 27 27 TYR J 15 LYS J 38 1 24
HELIX 28 28 SER J 43 HIS J 71 1 29
HELIX 29 29 ASN J 78 ALA J 86 1 9
HELIX 30 30 SER J 89 ALA J 104 1 16
HELIX 31 31 TYR K 15 LYS K 38 1 24
HELIX 32 32 SER K 43 ALA K 72 1 30
HELIX 33 33 ASN K 78 ALA K 86 1 9
HELIX 34 34 SER K 89 LYS K 114 1 26
HELIX 35 35 ARG L 11 HIS L 20 1 10
HELIX 36 36 SER L 31 GLU L 60 1 30
HELIX 37 37 ASP L 66 VAL L 73 1 8
HELIX 38 38 VAL L 73 PHE L 81 1 9
HELIX 39 39 ARG M 11 HIS M 20 1 10
HELIX 40 40 SER M 31 GLU M 60 1 30
HELIX 41 41 ASP M 66 PHE M 81 1 16
HELIX 42 42 ARG N 11 PHE N 23 1 13
HELIX 43 43 SER N 31 GLU N 60 1 30
HELIX 44 44 ASP N 66 PHE N 81 1 16
HELIX 45 45 TYR Q 15 ALA Q 39 1 25
HELIX 46 46 SER Q 43 HIS Q 71 1 29
HELIX 47 47 ASN Q 78 ALA Q 86 1 9
HELIX 48 48 SER Q 89 LYS Q 114 1 26
HELIX 49 49 TYR R 15 ALA R 39 1 25
HELIX 50 50 SER R 43 ALA R 72 1 30
HELIX 51 51 ASN R 78 ALA R 86 1 9
HELIX 52 52 SER R 89 GLN R 105 1 17
HELIX 53 53 TYR S 15 ALA S 39 1 25
HELIX 54 54 SER S 43 ALA S 72 1 30
HELIX 55 55 ASN S 78 ALA S 86 1 9
HELIX 56 56 SER S 89 ALA S 106 1 18
HELIX 57 57 TYR T 15 ALA T 39 1 25
HELIX 58 58 SER T 43 ALA T 72 1 30
HELIX 59 59 ASN T 78 ALA T 86 1 9
HELIX 60 60 SER T 89 LYS T 114 1 26
HELIX 61 61 ARG U 11 LEU U 21 1 11
HELIX 62 62 SER U 31 GLU U 60 1 30
HELIX 63 63 ASP U 66 PHE U 81 1 16
HELIX 64 64 ARG V 11 LEU V 21 1 11
HELIX 65 65 SER V 31 GLU V 60 1 30
HELIX 66 66 ASP V 66 PHE V 81 1 16
HELIX 67 67 ARG W 11 LEU W 21 1 11
HELIX 68 68 SER W 31 GLU W 60 1 30
HELIX 69 69 ASP W 66 PHE W 81 1 16
HELIX 70 70 ARG X 11 LEU X 21 1 11
HELIX 71 71 SER X 31 GLU X 60 1 30
HELIX 72 72 ASP X 66 PHE X 81 1 16
HELIX 73 73 TYR Y 15 ALA Y 39 1 25
HELIX 74 74 SER Y 43 ALA Y 72 1 30
HELIX 75 75 ASN Y 78 ALA Y 86 1 9
HELIX 76 76 SER Y 89 ALA Y 106 1 18
HELIX 77 77 ARG Z 11 LEU Z 21 1 11
HELIX 78 78 SER Z 31 GLU Z 60 1 30
HELIX 79 79 ASP Z 66 PHE Z 81 1 16
HELIX 80 80 TYR a 15 ALA a 39 1 25
HELIX 81 81 SER a 43 ALA a 72 1 30
HELIX 82 82 ASN a 78 ALA a 86 1 9
HELIX 83 83 SER a 89 ALA a 106 1 18
HELIX 84 84 ARG b 11 LEU b 21 1 11
HELIX 85 85 SER b 31 GLU b 60 1 30
HELIX 86 86 ASP b 66 PHE b 81 1 16
HELIX 87 87 TYR c 15 ALA c 39 1 25
HELIX 88 88 SER c 43 ALA c 72 1 30
HELIX 89 89 ASN c 78 ALA c 86 1 9
HELIX 90 90 SER c 89 GLN c 105 1 17
HELIX 91 91 ARG d 11 LEU d 21 1 11
HELIX 92 92 SER d 31 ASP d 61 1 31
HELIX 93 93 ASP d 66 PHE d 81 1 16
HELIX 94 94 TYR e 15 ALA e 39 1 25
HELIX 95 95 SER e 43 ALA e 72 1 30
HELIX 96 96 ASN e 78 ALA e 86 1 9
HELIX 97 97 SER e 89 LYS e 114 1 26
HELIX 98 98 TYR f 15 ALA f 39 1 25
HELIX 99 99 SER f 43 ALA f 72 1 30
HELIX 100 100 ASN f 78 ALA f 86 1 9
HELIX 101 101 SER f 89 GLN f 105 1 17
HELIX 102 102 TYR g 15 ALA g 39 1 25
HELIX 103 103 SER g 43 ALA g 72 1 30
HELIX 104 104 ASN g 78 ALA g 86 1 9
HELIX 105 105 SER g 89 LYS g 114 1 26
HELIX 106 106 ARG h 11 LEU h 21 1 11
HELIX 107 107 SER h 31 GLU h 60 1 30
HELIX 108 108 ASP h 66 PHE h 81 1 16
HELIX 109 109 ARG i 11 PHE i 23 1 13
HELIX 110 110 SER i 31 GLU i 60 1 30
HELIX 111 111 ASP i 66 PHE i 81 1 16
HELIX 112 112 ARG j 11 PHE j 23 1 13
HELIX 113 113 SER j 31 GLU j 60 1 30
HELIX 114 114 ASP j 66 PHE j 81 1 16
HELIX 115 115 TYR k 15 ALA k 39 1 25
HELIX 116 116 SER k 43 ALA k 72 1 30
HELIX 117 117 ASN k 78 ALA k 86 1 9
HELIX 118 118 SER k 89 LYS k 114 1 26
HELIX 119 119 TYR l 15 ALA l 39 1 25
HELIX 120 120 SER l 43 ALA l 72 1 30
HELIX 121 121 ASN l 78 ALA l 86 1 9
HELIX 122 122 SER l 89 GLN l 105 1 17
HELIX 123 123 TYR m 15 ALA m 39 1 25
HELIX 124 124 SER m 43 ALA m 72 1 30
HELIX 125 125 ASN m 78 ALA m 86 1 9
HELIX 126 126 SER m 89 ALA m 106 1 18
HELIX 127 127 TYR n 15 ALA n 39 1 25
HELIX 128 128 SER n 43 ALA n 72 1 30
HELIX 129 129 ASN n 78 ALA n 86 1 9
HELIX 130 130 SER n 89 LYS n 114 1 26
HELIX 131 131 ARG o 11 LEU o 21 1 11
HELIX 132 132 SER o 31 GLU o 60 1 30
HELIX 133 133 ASP o 66 PHE o 81 1 16
HELIX 134 134 ARG p 11 LEU p 21 1 11
HELIX 135 135 SER p 31 GLU p 60 1 30
HELIX 136 136 ASP p 66 PHE p 81 1 16
HELIX 137 137 ARG q 11 LEU q 21 1 11
HELIX 138 138 SER q 31 GLU q 60 1 30
HELIX 139 139 ASP q 66 PHE q 81 1 16
HELIX 140 140 ARG r 11 LEU r 21 1 11
HELIX 141 141 SER r 31 GLU r 60 1 30
HELIX 142 142 ASP r 66 PHE r 81 1 16
SHEET 1 A 2 THR C 76 ILE C 77 0
SHEET 2 A 2 LYS D 29 VAL D 30 1 O LYS D 29 N ILE C 77
SHEET 1 B 2 THR A 76 ILE A 77 0
SHEET 2 B 2 LYS B 29 VAL B 30 1 O LYS B 29 N ILE A 77
SHEET 1 C 2 THR Q 76 ILE Q 77 0
SHEET 2 C 2 LYS V 29 VAL V 30 1 O LYS V 29 N ILE Q 77
SHEET 1 D 2 THR R 76 ILE R 77 0
SHEET 2 D 2 LYS W 29 VAL W 30 1 O LYS W 29 N ILE R 77
SHEET 1 E 2 THR Y 76 ILE Y 77 0
SHEET 2 E 2 LYS Z 29 VAL Z 30 1 O LYS Z 29 N ILE Y 77
SHEET 1 F 2 THR a 76 ILE a 77 0
SHEET 2 F 2 LYS b 29 VAL b 30 1 O LYS b 29 N ILE a 77
SHEET 1 G 2 THR e 76 ILE e 77 0
SHEET 2 G 2 LYS i 29 VAL i 30 1 O LYS i 29 N ILE e 77
SHEET 1 H 2 THR g 76 ILE g 77 0
SHEET 2 H 2 LYS h 29 VAL h 30 1 O LYS h 29 N ILE g 77
SHEET 1 I 2 THR k 76 ILE k 77 0
SHEET 2 I 2 LYS p 29 VAL p 30 1 O LYS p 29 N ILE k 77
SHEET 1 J 2 THR l 76 ILE l 77 0
SHEET 2 J 2 LYS q 29 VAL q 30 1 O LYS q 29 N ILE l 77
SHEET 1 K 2 THR m 76 ILE m 77 0
SHEET 2 K 2 LYS r 29 VAL r 30 1 O LYS r 29 N ILE m 77
SHEET 1 L 2 THR n 76 ILE n 77 0
SHEET 2 L 2 LYS o 29 VAL o 30 1 O LYS o 29 N ILE n 77
CRYST1 252.390 252.390 131.360 90.00 90.00 120.00 P 3 60
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 0.003962 0.002288 0.000000 0.00000
SCALE2 0.000000 0.004575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007613 0.00000
(ATOM LINES ARE NOT SHOWN.)
END