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HEADER HYDROLASE 10-FEB-17 5N4C
TITLE PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 35MER
TITLE 2 HYDROLYSIS AND MACROCYCLIZATION SUBSTRATE - S577A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 3 ORGANISM_TAXID: 109633;
SOURCE 4 GENE: POPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PJ414;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 13 ORGANISM_TAXID: 109633
KEYWDS AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH
REVDAT 1 01-NOV-17 5N4C 0
JRNL AUTH C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES
JRNL TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-00862-4
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 155177
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 7959
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11265
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 612
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23876
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 1196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.03000
REMARK 3 B22 (A**2) : -3.17000
REMARK 3 B33 (A**2) : 1.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.326
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.657
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24561 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 22570 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 33376 ; 1.423 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 52005 ; 0.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3010 ; 6.124 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1188 ;34.053 ;24.217
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3897 ;13.302 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 122 ;14.672 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3526 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28178 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5892 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 12052 ; 1.118 ; 1.285
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 12051 ; 1.118 ; 1.285
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15046 ; 1.879 ; 1.921
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 15047 ; 1.879 ; 1.921
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12509 ; 1.414 ; 1.414
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 12509 ; 1.414 ; 1.414
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 18327 ; 2.293 ; 2.058
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 26032 ; 4.772 ;15.010
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 26032 ; 4.772 ;15.009
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 12
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 725 B 6 725 45522 0.06 0.05
REMARK 3 2 A 6 727 C 6 727 45592 0.06 0.05
REMARK 3 3 A 7 725 D 7 725 45396 0.06 0.05
REMARK 3 4 E 3 35 F 3 35 1456 0.08 0.05
REMARK 3 5 E 3 35 G 3 35 1536 0.09 0.05
REMARK 3 6 E 3 35 H 3 35 1538 0.07 0.05
REMARK 3 7 B 6 726 C 6 726 45578 0.07 0.05
REMARK 3 8 B 7 725 D 7 725 45420 0.06 0.05
REMARK 3 9 C 7 725 D 7 725 45460 0.06 0.05
REMARK 3 10 F 3 35 G 3 35 1470 0.08 0.05
REMARK 3 11 F 3 35 H 3 35 1502 0.04 0.05
REMARK 3 12 G 3 35 H 3 35 1620 0.07 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8060 6.3270 46.3790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0788 T22: 0.4341
REMARK 3 T33: 0.1434 T12: 0.0143
REMARK 3 T13: -0.0444 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.5422 L22: 1.4446
REMARK 3 L33: 1.6074 L12: -0.0795
REMARK 3 L13: -0.2617 L23: -0.9031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: -0.1296 S13: -0.1590
REMARK 3 S21: 0.0226 S22: -0.0669 S23: -0.2067
REMARK 3 S31: 0.2079 S32: 0.2787 S33: 0.1136
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 : A 83 A 450
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4940 41.8440 45.8280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.2886
REMARK 3 T33: 0.0916 T12: 0.0168
REMARK 3 T13: 0.0173 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.2319 L22: 0.5622
REMARK 3 L33: 0.9955 L12: 0.0762
REMARK 3 L13: -0.0411 L23: 0.1050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0476 S12: -0.1204 S13: 0.1186
REMARK 3 S21: -0.0092 S22: 0.0022 S23: -0.0494
REMARK 3 S31: -0.1225 S32: 0.0321 S33: -0.0499
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 : A 451 A 696
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9070 10.9870 39.4650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: 0.3004
REMARK 3 T33: 0.0703 T12: 0.0034
REMARK 3 T13: -0.0263 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9108 L22: 0.8050
REMARK 3 L33: 1.7749 L12: -0.1622
REMARK 3 L13: -0.0489 L23: -0.3824
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: -0.0401 S13: -0.0398
REMARK 3 S21: 0.0780 S22: 0.0627 S23: 0.0041
REMARK 3 S31: 0.0000 S32: -0.0293 S33: -0.0599
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 : A 697 A 727
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8700 15.9120 32.5830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0733 T22: 0.3311
REMARK 3 T33: 0.0941 T12: 0.0184
REMARK 3 T13: -0.0032 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.8794 L22: 5.3366
REMARK 3 L33: 1.5165 L12: 1.1542
REMARK 3 L13: 0.7876 L23: 1.6346
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0324 S13: -0.0954
REMARK 3 S21: -0.0184 S22: 0.0289 S23: -0.0330
REMARK 3 S31: -0.0735 S32: 0.0103 S33: -0.0053
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 : B 6 B 133
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0700 45.4790 -17.1140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0170 T22: 0.3504
REMARK 3 T33: 0.0844 T12: -0.0135
REMARK 3 T13: 0.0260 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 1.0136 L22: 1.4466
REMARK 3 L33: 0.7272 L12: -0.0560
REMARK 3 L13: 0.1799 L23: 0.2597
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: -0.0506 S13: 0.0250
REMARK 3 S21: -0.0060 S22: 0.0450 S23: 0.2107
REMARK 3 S31: -0.0628 S32: -0.1186 S33: -0.0937
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 134 B 449
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7920 27.3030 -10.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0059 T22: 0.2880
REMARK 3 T33: 0.1120 T12: 0.0056
REMARK 3 T13: -0.0163 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.3911 L22: 0.7180
REMARK 3 L33: 0.9982 L12: 0.0299
REMARK 3 L13: 0.1514 L23: -0.1595
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: -0.1849 S13: -0.1739
REMARK 3 S21: 0.0157 S22: -0.0035 S23: 0.0827
REMARK 3 S31: 0.0338 S32: -0.0451 S33: -0.0599
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 : B 450 B 693
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6030 57.3890 -18.6190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0280 T22: 0.2643
REMARK 3 T33: 0.1034 T12: -0.0060
REMARK 3 T13: 0.0413 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.1133 L22: 0.7173
REMARK 3 L33: 1.4937 L12: -0.0991
REMARK 3 L13: 0.0577 L23: 0.1781
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: -0.0352 S13: 0.1640
REMARK 3 S21: 0.0702 S22: 0.0750 S23: 0.0490
REMARK 3 S31: -0.1095 S32: 0.0278 S33: -0.0848
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 : B 694 B 726
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9210 51.6820 -22.7510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0879 T22: 0.3342
REMARK 3 T33: 0.1258 T12: 0.0265
REMARK 3 T13: -0.0017 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 2.7397 L22: 4.5495
REMARK 3 L33: 0.4228 L12: 0.7959
REMARK 3 L13: 0.1482 L23: 0.4576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: -0.1489 S13: 0.0568
REMARK 3 S21: 0.2414 S22: 0.0407 S23: 0.0313
REMARK 3 S31: 0.0127 S32: 0.0186 S33: -0.0559
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 : C 6 C 108
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8230 51.5720 25.7320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0222 T22: 0.3739
REMARK 3 T33: 0.0995 T12: 0.0433
REMARK 3 T13: 0.0235 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.9947 L22: 1.3622
REMARK 3 L33: 0.6110 L12: 0.3001
REMARK 3 L13: 0.3033 L23: -0.4657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: 0.1140 S13: 0.0066
REMARK 3 S21: -0.0562 S22: 0.0166 S23: -0.2192
REMARK 3 S31: -0.0251 S32: 0.1248 S33: -0.0154
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 : C 109 C 451
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8620 26.6060 22.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0242 T22: 0.3029
REMARK 3 T33: 0.1136 T12: 0.0122
REMARK 3 T13: -0.0414 T23: -0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 1.2156 L22: 0.7083
REMARK 3 L33: 0.9571 L12: 0.0729
REMARK 3 L13: 0.2816 L23: 0.2719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0946 S12: 0.1565 S13: -0.2242
REMARK 3 S21: 0.0461 S22: 0.0130 S23: -0.1145
REMARK 3 S31: 0.0971 S32: 0.0901 S33: -0.1077
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 : C 452 C 700
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3370 56.8120 29.1460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0059 T22: 0.2541
REMARK 3 T33: 0.0606 T12: 0.0172
REMARK 3 T13: 0.0084 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.0207 L22: 0.8550
REMARK 3 L33: 1.4840 L12: 0.3774
REMARK 3 L13: -0.0860 L23: -0.2704
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.0614 S13: 0.0195
REMARK 3 S21: -0.0450 S22: 0.0274 S23: -0.0257
REMARK 3 S31: 0.0506 S32: 0.0107 S33: -0.0090
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 : C 701 C 728
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6710 53.7750 38.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0409 T22: 0.2451
REMARK 3 T33: 0.1054 T12: -0.0133
REMARK 3 T13: -0.0147 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 3.3807 L22: 9.4042
REMARK 3 L33: 1.4043 L12: -3.5249
REMARK 3 L13: -0.8630 L23: 1.4473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0379 S12: -0.1093 S13: 0.1467
REMARK 3 S21: 0.0963 S22: 0.0907 S23: -0.1802
REMARK 3 S31: 0.0112 S32: 0.0355 S33: -0.1287
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 : D 7 D 117
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9570 20.4740 84.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0342 T22: 0.4048
REMARK 3 T33: 0.0607 T12: 0.0136
REMARK 3 T13: -0.0340 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.7532 L22: 1.3794
REMARK 3 L33: 0.8389 L12: 0.1035
REMARK 3 L13: -0.0329 L23: 0.2433
REMARK 3 S TENSOR
REMARK 3 S11: 0.0571 S12: 0.0797 S13: -0.0508
REMARK 3 S21: -0.0713 S22: -0.0008 S23: 0.1551
REMARK 3 S31: 0.1173 S32: -0.0688 S33: -0.0563
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 : D 118 D 448
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9730 41.9790 79.4240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: 0.3061
REMARK 3 T33: 0.0699 T12: -0.0148
REMARK 3 T13: 0.0085 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 1.1031 L22: 0.7264
REMARK 3 L33: 0.9877 L12: -0.0817
REMARK 3 L13: 0.0027 L23: -0.0978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0358 S12: 0.1299 S13: 0.1115
REMARK 3 S21: -0.0364 S22: -0.0212 S23: 0.0401
REMARK 3 S31: -0.0485 S32: -0.0222 S33: -0.0146
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 : D 449 D 693
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4760 11.8560 87.8460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0329 T22: 0.2873
REMARK 3 T33: 0.0617 T12: 0.0181
REMARK 3 T13: -0.0251 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.0481 L22: 0.7912
REMARK 3 L33: 1.6025 L12: 0.2257
REMARK 3 L13: 0.1447 L23: 0.2166
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: 0.0701 S13: -0.0821
REMARK 3 S21: -0.1096 S22: 0.0239 S23: 0.0291
REMARK 3 S31: 0.1001 S32: 0.0531 S33: -0.0606
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 : D 694 D 726
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0070 17.4760 91.6730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0149 T22: 0.2989
REMARK 3 T33: 0.1127 T12: -0.0162
REMARK 3 T13: 0.0126 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 2.5087 L22: 7.6658
REMARK 3 L33: 2.1262 L12: -1.2764
REMARK 3 L13: 1.1466 L23: -2.1714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.1384 S13: -0.0326
REMARK 3 S21: -0.2352 S22: -0.0018 S23: 0.1633
REMARK 3 S31: 0.0697 S32: 0.0368 S33: -0.0221
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 : E 3 E 18
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5830 27.0000 47.1990
REMARK 3 T TENSOR
REMARK 3 T11: 0.4465 T22: 0.5678
REMARK 3 T33: 0.4010 T12: 0.0768
REMARK 3 T13: 0.0502 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 2.0267 L22: 7.0006
REMARK 3 L33: 2.6478 L12: 0.7962
REMARK 3 L13: 2.1333 L23: 2.4490
REMARK 3 S TENSOR
REMARK 3 S11: -0.2554 S12: 0.0530 S13: 0.4527
REMARK 3 S21: -0.3863 S22: -0.0613 S23: -0.0953
REMARK 3 S31: -0.3305 S32: 0.0658 S33: 0.3167
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 : E 19 E 25
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4500 23.9030 35.8910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2922 T22: 0.5699
REMARK 3 T33: 0.3790 T12: -0.0348
REMARK 3 T13: 0.0828 T23: -0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 1.7950 L22: 13.5853
REMARK 3 L33: 3.2779 L12: -4.4228
REMARK 3 L13: 1.9412 L23: -3.0052
REMARK 3 S TENSOR
REMARK 3 S11: 0.3446 S12: 0.1965 S13: 0.2884
REMARK 3 S21: -0.7924 S22: -0.4537 S23: -0.9609
REMARK 3 S31: 0.4563 S32: 0.2771 S33: 0.1091
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 : E 26 E 35
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9360 39.3330 37.9140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0946 T22: 0.2680
REMARK 3 T33: 0.0945 T12: 0.0371
REMARK 3 T13: 0.0209 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 6.4742 L22: 10.9314
REMARK 3 L33: 8.4127 L12: -1.8993
REMARK 3 L13: -3.3146 L23: 7.3855
REMARK 3 S TENSOR
REMARK 3 S11: -0.4157 S12: 0.0283 S13: -0.0840
REMARK 3 S21: 0.8684 S22: 0.0826 S23: 0.2441
REMARK 3 S31: 0.5954 S32: -0.1784 S33: 0.3332
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 : F 2 F 11
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1250 40.4570 -8.3220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3410 T22: 0.4904
REMARK 3 T33: 0.4085 T12: -0.0005
REMARK 3 T13: 0.1415 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 4.2464 L22: 14.4024
REMARK 3 L33: 3.2699 L12: -3.0354
REMARK 3 L13: 2.0329 L23: 2.9874
REMARK 3 S TENSOR
REMARK 3 S11: -0.1589 S12: -0.0652 S13: -0.8734
REMARK 3 S21: -0.2179 S22: 0.5463 S23: -0.0119
REMARK 3 S31: 0.2231 S32: 0.2456 S33: -0.3874
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 : F 12 F 25
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2010 43.7440 -19.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2598 T22: 0.5876
REMARK 3 T33: 0.5376 T12: -0.0767
REMARK 3 T13: -0.0357 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 2.8472 L22: 13.8206
REMARK 3 L33: 8.7098 L12: 2.3306
REMARK 3 L13: -3.8789 L23: 3.2016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: 0.2648 S13: -0.0960
REMARK 3 S21: 0.5126 S22: -0.4055 S23: 0.4495
REMARK 3 S31: 0.0445 S32: -0.6609 S33: 0.3079
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 : F 26 F 35
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3900 29.2360 -20.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2022 T22: 0.3189
REMARK 3 T33: 0.1816 T12: -0.0544
REMARK 3 T13: -0.0208 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 2.4821 L22: 7.6332
REMARK 3 L33: 7.1458 L12: -2.4792
REMARK 3 L13: 4.0406 L23: -5.0734
REMARK 3 S TENSOR
REMARK 3 S11: -0.1807 S12: -0.0301 S13: 0.1465
REMARK 3 S21: 0.4984 S22: -0.1076 S23: -0.0613
REMARK 3 S31: -0.5418 S32: 0.2814 S33: 0.2883
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 : G 3 G 11
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3090 40.9090 18.5580
REMARK 3 T TENSOR
REMARK 3 T11: 0.3567 T22: 0.4863
REMARK 3 T33: 0.2485 T12: -0.0471
REMARK 3 T13: 0.0319 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.0914 L22: 16.5768
REMARK 3 L33: 2.1792 L12: 1.1423
REMARK 3 L13: 1.2763 L23: -1.8303
REMARK 3 S TENSOR
REMARK 3 S11: 0.2299 S12: -0.0270 S13: -0.0690
REMARK 3 S21: 0.1600 S22: 0.0053 S23: 0.5729
REMARK 3 S31: 0.4152 S32: -0.1226 S33: -0.2353
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 : G 12 G 25
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6600 42.4160 30.0700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2327 T22: 0.5693
REMARK 3 T33: 0.5161 T12: -0.0240
REMARK 3 T13: 0.0152 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 3.3687 L22: 14.9041
REMARK 3 L33: 5.3659 L12: -5.0846
REMARK 3 L13: -0.4735 L23: -2.7698
REMARK 3 S TENSOR
REMARK 3 S11: -0.2230 S12: 0.0410 S13: -0.3563
REMARK 3 S21: -0.3163 S22: 0.1635 S23: -0.3126
REMARK 3 S31: 0.3027 S32: -0.1640 S33: 0.0595
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 : G 26 G 35
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5180 28.7640 31.0820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1325 T22: 0.2630
REMARK 3 T33: 0.1553 T12: 0.0345
REMARK 3 T13: -0.0535 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 7.4417 L22: 6.8486
REMARK 3 L33: 7.2319 L12: 2.6205
REMARK 3 L13: 4.2440 L23: 5.6217
REMARK 3 S TENSOR
REMARK 3 S11: -0.1144 S12: -0.0380 S13: 0.1596
REMARK 3 S21: -0.5447 S22: -0.1447 S23: 0.1370
REMARK 3 S31: -0.4112 S32: -0.2594 S33: 0.2591
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 : H 3 H 11
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9020 27.6960 76.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.5202 T22: 0.5628
REMARK 3 T33: 0.2169 T12: -0.0947
REMARK 3 T13: -0.1684 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 11.4979 L22: 0.7397
REMARK 3 L33: 3.1529 L12: -2.9041
REMARK 3 L13: -6.0016 L23: 1.5267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0292 S12: -0.3112 S13: 0.4188
REMARK 3 S21: -0.0566 S22: 0.1236 S23: -0.0831
REMARK 3 S31: -0.0918 S32: 0.2250 S33: -0.1528
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 : H 12 H 25
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5460 26.2520 88.0530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3752 T22: 0.6328
REMARK 3 T33: 0.6540 T12: 0.0347
REMARK 3 T13: 0.1192 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 5.6958 L22: 12.7249
REMARK 3 L33: 1.3702 L12: -2.6338
REMARK 3 L13: 1.0762 L23: 3.0601
REMARK 3 S TENSOR
REMARK 3 S11: -0.2001 S12: -0.5008 S13: 0.3747
REMARK 3 S21: -1.2799 S22: 0.1793 S23: 0.4425
REMARK 3 S31: -0.5341 S32: -0.1449 S33: 0.0208
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 : H 26 H 35
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7560 40.0620 89.0280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1239 T22: 0.3149
REMARK 3 T33: 0.1956 T12: 0.0217
REMARK 3 T13: 0.0201 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 4.9318 L22: 10.5207
REMARK 3 L33: 7.8593 L12: 5.2419
REMARK 3 L13: -2.6738 L23: -8.3692
REMARK 3 S TENSOR
REMARK 3 S11: -0.3122 S12: 0.0651 S13: -0.1811
REMARK 3 S21: -0.3653 S22: 0.0582 S23: -0.4780
REMARK 3 S31: 0.2450 S32: -0.2092 S33: 0.2540
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5N4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003495.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 163136
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 90.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
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 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 (%): 49.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000, 100 MM BICINE PH 8.7, 64
REMARK 280 MM SODIUM POTASSIUM PHOSPHATE, 12.5MM HEXAMMINE COBALT CHLORIDE,
REMARK 280 CRYSTALS CRYOPROTECTED WITH 12% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 71.28100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 GLU A 226
REMARK 465 GLY A 227
REMARK 465 THR A 728
REMARK 465 VAL A 729
REMARK 465 GLU A 730
REMARK 465 MET E 1
REMARK 465 PHE E 2
REMARK 465 ILE E 14
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 LYS B 727
REMARK 465 THR B 728
REMARK 465 VAL B 729
REMARK 465 GLU B 730
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 VAL C 4
REMARK 465 THR C 5
REMARK 465 VAL C 189
REMARK 465 ASP C 190
REMARK 465 VAL C 729
REMARK 465 GLU C 730
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 SER D 3
REMARK 465 VAL D 4
REMARK 465 THR D 5
REMARK 465 TRP D 6
REMARK 465 LYS D 727
REMARK 465 THR D 728
REMARK 465 VAL D 729
REMARK 465 GLU D 730
REMARK 465 MET F 1
REMARK 465 GLY F 15
REMARK 465 CYS F 16
REMARK 465 MET G 1
REMARK 465 PHE G 2
REMARK 465 MET H 1
REMARK 465 PHE H 2
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 F 2 CG CD1 CD2 CE1 CE2 CZ
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 OG1 THR B 244 OE1 GLU B 246 1.72
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 O PRO A 115 NE2 GLN D 682 2556 1.80
REMARK 500 O ASP B 18 NZ LYS D 564 2556 2.04
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 16 CA - CB - SG ANGL. DEV. = 7.3 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 THR A 5 115.24 -161.88
REMARK 500 ASP A 280 -166.41 -172.88
REMARK 500 ALA A 311 -31.84 -148.44
REMARK 500 ILE A 317 -60.28 -93.17
REMARK 500 ALA A 332 79.25 -156.24
REMARK 500 TYR A 335 159.76 75.27
REMARK 500 GLU A 369 -45.19 72.96
REMARK 500 THR A 439 -17.14 91.17
REMARK 500 GLU A 452 -58.25 70.30
REMARK 500 ARG A 543 -120.42 49.19
REMARK 500 ALA A 577 -106.25 59.75
REMARK 500 ALA A 605 -37.79 -152.31
REMARK 500 THR A 614 -125.31 39.16
REMARK 500 MET A 667 -50.76 -27.46
REMARK 500 VAL E 24 -43.81 -29.03
REMARK 500 ASP B 280 -166.94 -172.51
REMARK 500 ALA B 311 -32.39 -148.25
REMARK 500 ILE B 317 -60.31 -92.81
REMARK 500 ALA B 332 80.18 -155.54
REMARK 500 TYR B 335 160.59 75.10
REMARK 500 GLU B 369 -45.14 73.24
REMARK 500 THR B 439 -16.66 91.12
REMARK 500 GLU B 452 -60.02 71.44
REMARK 500 ARG B 543 -121.14 50.47
REMARK 500 ALA B 577 -106.19 59.49
REMARK 500 ALA B 605 -38.28 -151.04
REMARK 500 THR B 614 -125.45 39.19
REMARK 500 MET B 667 -51.04 -27.39
REMARK 500 ASP C 280 -168.88 -172.90
REMARK 500 ALA C 311 -32.64 -148.43
REMARK 500 ALA C 332 79.51 -156.50
REMARK 500 TYR C 335 160.80 74.85
REMARK 500 GLU C 369 -45.43 73.36
REMARK 500 GLU C 452 -58.29 70.57
REMARK 500 ARG C 543 -119.43 48.78
REMARK 500 ALA C 577 -105.41 58.79
REMARK 500 ALA C 605 -37.95 -151.06
REMARK 500 THR C 614 -124.21 38.08
REMARK 500 MET C 667 -50.54 -28.38
REMARK 500 THR D 228 -168.28 -113.00
REMARK 500 ASP D 280 -168.55 -173.12
REMARK 500 ALA D 311 -31.93 -147.94
REMARK 500 ALA D 332 79.71 -156.48
REMARK 500 TYR D 335 160.69 75.29
REMARK 500 GLU D 369 -45.89 73.59
REMARK 500 THR D 439 -17.77 91.81
REMARK 500 GLU D 452 -58.08 69.72
REMARK 500 ARG D 543 -120.05 50.66
REMARK 500 ALA D 577 -106.23 59.53
REMARK 500 ALA D 605 -37.94 -152.01
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1089 DISTANCE = 5.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 801
DBREF 5N4C A 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4C E 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
DBREF 5N4C B 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4C C 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4C D 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4C F 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
DBREF 5N4C G 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
DBREF 5N4C H 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
SEQADV 5N4C ALA A 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQADV 5N4C ALA B 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQADV 5N4C ALA C 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQADV 5N4C ALA D 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQRES 1 A 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 A 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 A 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 A 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 A 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 A 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 A 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 A 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 A 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 A 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 A 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 A 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 A 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 A 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 A 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 A 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 A 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 A 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 A 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 A 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 A 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 A 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 A 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 A 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 A 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 A 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 A 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 A 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 A 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 A 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 A 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 A 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 A 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 A 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 A 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 A 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 A 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 A 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 A 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 A 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 A 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 A 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 A 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 A 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 A 730 ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 A 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 A 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 A 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 A 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 A 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 A 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 A 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 A 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 A 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 A 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 A 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 A 730 VAL GLU
SEQRES 1 E 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 E 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 E 35 THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 B 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 B 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 B 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 B 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 B 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 B 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 B 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 B 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 B 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 B 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 B 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 B 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 B 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 B 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 B 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 B 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 B 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 B 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 B 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 B 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 B 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 B 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 B 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 B 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 B 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 B 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 B 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 B 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 B 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 B 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 B 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 B 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 B 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 B 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 B 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 B 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 B 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 B 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 B 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 B 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 B 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 B 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 B 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 B 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 B 730 ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 B 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 B 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 B 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 B 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 B 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 B 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 B 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 B 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 B 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 B 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 B 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 B 730 VAL GLU
SEQRES 1 C 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 C 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 C 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 C 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 C 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 C 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 C 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 C 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 C 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 C 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 C 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 C 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 C 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 C 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 C 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 C 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 C 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 C 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 C 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 C 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 C 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 C 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 C 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 C 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 C 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 C 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 C 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 C 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 C 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 C 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 C 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 C 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 C 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 C 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 C 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 C 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 C 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 C 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 C 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 C 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 C 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 C 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 C 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 C 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 C 730 ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 C 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 C 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 C 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 C 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 C 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 C 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 C 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 C 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 C 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 C 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 C 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 C 730 VAL GLU
SEQRES 1 D 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 D 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 D 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 D 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 D 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 D 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 D 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 D 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 D 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 D 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 D 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 D 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 D 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 D 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 D 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 D 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 D 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 D 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 D 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 D 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 D 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 D 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 D 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 D 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 D 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 D 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 D 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 D 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 D 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 D 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 D 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 D 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 D 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 D 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 D 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 D 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 D 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 D 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 D 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 D 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 D 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 D 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 D 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 D 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 D 730 ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 D 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 D 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 D 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 D 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 D 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 D 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 D 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 D 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 D 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 D 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 D 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 D 730 VAL GLU
SEQRES 1 F 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 F 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 F 35 THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 G 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 G 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 G 35 THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 H 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 H 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 H 35 THR LEU ALA SER GLY ASN ASP ILE CYS
HET GOL D 801 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *1196(H2 O)
HELIX 1 AA1 TYR A 37 GLU A 42 5 6
HELIX 2 AA2 THR A 44 GLN A 64 1 21
HELIX 3 AA3 ALA A 66 ASN A 80 1 15
HELIX 4 AA4 ASP A 119 LYS A 122 5 4
HELIX 5 AA5 GLY A 123 VAL A 127 1 5
HELIX 6 AA6 ASP A 133 LEU A 137 5 5
HELIX 7 AA7 SER A 181 GLY A 188 1 8
HELIX 8 AA8 THR A 244 ASP A 248 5 5
HELIX 9 AA9 ASP A 454 ASP A 456 5 3
HELIX 10 AB1 SER A 508 GLY A 519 1 12
HELIX 11 AB2 GLY A 534 GLY A 540 1 7
HELIX 12 AB3 GLY A 541 THR A 545 5 5
HELIX 13 AB4 LYS A 546 ASN A 563 1 18
HELIX 14 AB5 ALA A 577 ALA A 590 1 14
HELIX 15 AB6 LYS A 609 PHE A 613 5 5
HELIX 16 AB7 GLY A 615 ALA A 618 5 4
HELIX 17 AB8 TRP A 619 GLY A 624 1 6
HELIX 18 AB9 ILE A 628 TYR A 636 1 9
HELIX 19 AC1 SER A 639 ASN A 643 5 5
HELIX 20 AC2 PRO A 666 VAL A 680 1 15
HELIX 21 AC3 PRO A 703 LEU A 722 1 20
HELIX 22 AC4 THR E 4 LEU E 9 5 6
HELIX 23 AC5 THR E 20 ASP E 25 5 6
HELIX 24 AC6 TYR B 37 GLU B 42 5 6
HELIX 25 AC7 THR B 44 GLN B 64 1 21
HELIX 26 AC8 ALA B 66 ASN B 80 1 15
HELIX 27 AC9 ASP B 119 LYS B 122 5 4
HELIX 28 AD1 GLY B 123 VAL B 127 1 5
HELIX 29 AD2 ASP B 133 LEU B 137 5 5
HELIX 30 AD3 SER B 181 GLY B 188 1 8
HELIX 31 AD4 THR B 244 ASP B 248 5 5
HELIX 32 AD5 ASP B 454 ASP B 456 5 3
HELIX 33 AD6 SER B 508 GLY B 519 1 12
HELIX 34 AD7 GLY B 534 GLY B 540 1 7
HELIX 35 AD8 GLY B 541 THR B 545 5 5
HELIX 36 AD9 LYS B 546 ASN B 563 1 18
HELIX 37 AE1 ALA B 577 ALA B 590 1 14
HELIX 38 AE2 LYS B 609 PHE B 613 5 5
HELIX 39 AE3 GLY B 615 ALA B 618 5 4
HELIX 40 AE4 TRP B 619 GLY B 624 1 6
HELIX 41 AE5 ILE B 628 TYR B 636 1 9
HELIX 42 AE6 SER B 639 ASN B 643 5 5
HELIX 43 AE7 PRO B 666 VAL B 680 1 15
HELIX 44 AE8 PRO B 703 LEU B 722 1 20
HELIX 45 AE9 TYR C 37 GLU C 42 5 6
HELIX 46 AF1 THR C 44 GLN C 64 1 21
HELIX 47 AF2 ALA C 66 ASN C 80 1 15
HELIX 48 AF3 ASP C 119 LYS C 122 5 4
HELIX 49 AF4 GLY C 123 VAL C 127 1 5
HELIX 50 AF5 ASP C 133 LEU C 137 5 5
HELIX 51 AF6 SER C 181 GLY C 188 1 8
HELIX 52 AF7 THR C 244 ASP C 248 5 5
HELIX 53 AF8 PRO C 437 GLN C 440 5 4
HELIX 54 AF9 ASP C 454 ASP C 456 5 3
HELIX 55 AG1 SER C 508 GLY C 519 1 12
HELIX 56 AG2 GLY C 534 GLY C 540 1 7
HELIX 57 AG3 GLY C 541 THR C 545 5 5
HELIX 58 AG4 LYS C 546 ASN C 563 1 18
HELIX 59 AG5 ALA C 577 ALA C 590 1 14
HELIX 60 AG6 LYS C 609 PHE C 613 5 5
HELIX 61 AG7 GLY C 615 ALA C 618 5 4
HELIX 62 AG8 TRP C 619 GLY C 624 1 6
HELIX 63 AG9 ILE C 628 TYR C 636 1 9
HELIX 64 AH1 SER C 639 ASN C 643 5 5
HELIX 65 AH2 PRO C 666 VAL C 680 1 15
HELIX 66 AH3 PRO C 703 LEU C 722 1 20
HELIX 67 AH4 TYR D 37 GLU D 42 5 6
HELIX 68 AH5 THR D 44 GLN D 64 1 21
HELIX 69 AH6 ALA D 66 ASN D 80 1 15
HELIX 70 AH7 ASP D 119 LYS D 122 5 4
HELIX 71 AH8 GLY D 123 VAL D 127 1 5
HELIX 72 AH9 ASP D 133 LEU D 137 5 5
HELIX 73 AI1 SER D 181 GLY D 188 1 8
HELIX 74 AI2 THR D 244 ASP D 248 5 5
HELIX 75 AI3 ASP D 454 ASP D 456 5 3
HELIX 76 AI4 SER D 508 GLY D 519 1 12
HELIX 77 AI5 GLY D 534 GLY D 540 1 7
HELIX 78 AI6 GLY D 541 THR D 545 5 5
HELIX 79 AI7 LYS D 546 ASN D 563 1 18
HELIX 80 AI8 ALA D 577 ALA D 590 1 14
HELIX 81 AI9 LYS D 609 PHE D 613 5 5
HELIX 82 AJ1 GLY D 615 ALA D 618 5 4
HELIX 83 AJ2 TRP D 619 GLY D 624 1 6
HELIX 84 AJ3 ILE D 628 TYR D 636 1 9
HELIX 85 AJ4 SER D 639 ASN D 643 5 5
HELIX 86 AJ5 PRO D 666 VAL D 680 1 15
HELIX 87 AJ6 PRO D 703 LEU D 722 1 20
HELIX 88 AJ7 THR F 4 LEU F 9 5 6
HELIX 89 AJ8 THR F 20 ASP F 25 5 6
HELIX 90 AJ9 THR G 4 LEU G 9 5 6
HELIX 91 AK1 THR G 20 ASP G 25 5 6
HELIX 92 AK2 THR H 4 LEU H 9 5 6
HELIX 93 AK3 THR H 20 ASP H 25 5 6
SHEET 1 AA1 2 VAL A 20 SER A 25 0
SHEET 2 AA1 2 GLY A 29 PRO A 34 -1 O VAL A 33 N ASP A 21
SHEET 1 AA2 3 LYS A 83 PHE A 84 0
SHEET 2 AA2 3 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA2 3 THR A 88 LEU A 89 -1 N THR A 88 O TYR A 96
SHEET 1 AA3 4 LYS A 83 PHE A 84 0
SHEET 2 AA3 4 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA3 4 VAL A 108 SER A 112 -1 O TYR A 110 N TRP A 97
SHEET 4 AA3 4 GLY A 128 PHE A 132 -1 O ASP A 129 N ARG A 111
SHEET 1 AA4 4 ALA A 143 PHE A 150 0
SHEET 2 AA4 4 PHE A 156 HIS A 163 -1 O ALA A 160 N LEU A 147
SHEET 3 AA4 4 SER A 169 SER A 175 -1 O THR A 170 N VAL A 161
SHEET 4 AA4 4 VAL A 197 PHE A 200 -1 O VAL A 197 N ILE A 171
SHEET 1 AA5 4 ILE A 206 TRP A 207 0
SHEET 2 AA5 4 GLY A 213 ARG A 218 -1 O LEU A 215 N ILE A 206
SHEET 3 AA5 4 MET A 235 LYS A 240 -1 O CYS A 237 N TYR A 216
SHEET 4 AA5 4 ILE A 249 TYR A 252 -1 O TYR A 252 N MET A 236
SHEET 1 AA6 4 ILE A 261 THR A 266 0
SHEET 2 AA6 4 TYR A 272 PHE A 278 -1 O TYR A 274 N ASP A 265
SHEET 3 AA6 4 LEU A 286 GLU A 291 -1 O ALA A 290 N LEU A 273
SHEET 4 AA6 4 ARG A 304 VAL A 307 -1 O ARG A 304 N VAL A 289
SHEET 1 AA7 4 TYR A 314 HIS A 320 0
SHEET 2 AA7 4 LEU A 323 THR A 328 -1 O TYR A 325 N ILE A 317
SHEET 3 AA7 4 LYS A 336 ASP A 341 -1 O ILE A 338 N ILE A 326
SHEET 4 AA7 4 GLU A 348 ILE A 353 -1 O PHE A 352 N VAL A 337
SHEET 1 AA8 4 LYS A 360 ALA A 367 0
SHEET 2 AA8 4 TYR A 371 ARG A 378 -1 O ILE A 375 N GLN A 363
SHEET 3 AA8 4 LYS A 381 TYR A 387 -1 O TYR A 387 N PHE A 372
SHEET 4 AA8 4 GLN A 393 LEU A 397 -1 O LEU A 394 N LEU A 386
SHEET 1 AA9 4 ALA A 404 ALA A 408 0
SHEET 2 AA9 4 HIS A 415 GLY A 422 -1 O PHE A 417 N ALA A 408
SHEET 3 AA9 4 THR A 425 ASP A 433 -1 O ALA A 430 N LEU A 418
SHEET 4 AA9 4 PHE A 442 THR A 447 -1 O SER A 443 N ARG A 431
SHEET 1 AB1 8 PHE A 458 GLU A 466 0
SHEET 2 AB1 8 LYS A 472 HIS A 480 -1 O ILE A 473 N TYR A 465
SHEET 3 AB1 8 ILE A 521 PRO A 525 -1 O PHE A 522 N VAL A 478
SHEET 4 AB1 8 ALA A 491 TYR A 494 1 N ILE A 492 O ILE A 521
SHEET 5 AB1 8 VAL A 571 ALA A 576 1 O ALA A 572 N GLN A 493
SHEET 6 AB1 8 ALA A 597 GLU A 601 1 O GLU A 601 N GLY A 575
SHEET 7 AB1 8 ALA A 652 ASN A 658 1 O LEU A 654 N ALA A 598
SHEET 8 AB1 8 LEU A 687 ASP A 692 1 O LYS A 690 N ILE A 655
SHEET 1 AB2 2 VAL B 20 SER B 25 0
SHEET 2 AB2 2 GLY B 29 PRO B 34 -1 O VAL B 33 N ASP B 21
SHEET 1 AB3 3 LYS B 83 PHE B 84 0
SHEET 2 AB3 3 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB3 3 THR B 88 LEU B 89 -1 N THR B 88 O TYR B 96
SHEET 1 AB4 4 LYS B 83 PHE B 84 0
SHEET 2 AB4 4 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB4 4 VAL B 108 SER B 112 -1 O TYR B 110 N TRP B 97
SHEET 4 AB4 4 GLY B 128 PHE B 132 -1 O PHE B 131 N LEU B 109
SHEET 1 AB5 4 ALA B 143 PHE B 150 0
SHEET 2 AB5 4 PHE B 156 HIS B 163 -1 O ALA B 160 N LEU B 147
SHEET 3 AB5 4 SER B 169 SER B 175 -1 O THR B 170 N VAL B 161
SHEET 4 AB5 4 VAL B 197 PHE B 200 -1 O VAL B 197 N ILE B 171
SHEET 1 AB6 4 ILE B 206 TRP B 207 0
SHEET 2 AB6 4 GLY B 213 ARG B 218 -1 O LEU B 215 N ILE B 206
SHEET 3 AB6 4 MET B 235 LYS B 240 -1 O HIS B 239 N PHE B 214
SHEET 4 AB6 4 ILE B 249 TYR B 252 -1 O TYR B 252 N MET B 236
SHEET 1 AB7 4 ILE B 261 THR B 266 0
SHEET 2 AB7 4 TYR B 272 PHE B 278 -1 O TYR B 274 N ASP B 265
SHEET 3 AB7 4 LEU B 286 GLU B 291 -1 O ALA B 290 N LEU B 273
SHEET 4 AB7 4 ARG B 304 VAL B 307 -1 O VAL B 307 N LEU B 287
SHEET 1 AB8 4 TYR B 314 HIS B 320 0
SHEET 2 AB8 4 LEU B 323 THR B 328 -1 O TYR B 325 N ILE B 317
SHEET 3 AB8 4 LYS B 336 ASP B 341 -1 O ILE B 338 N ILE B 326
SHEET 4 AB8 4 GLU B 348 ILE B 353 -1 O PHE B 352 N VAL B 337
SHEET 1 AB9 4 LYS B 360 ALA B 367 0
SHEET 2 AB9 4 TYR B 371 ARG B 378 -1 O VAL B 373 N ASN B 365
SHEET 3 AB9 4 LYS B 381 TYR B 387 -1 O TYR B 387 N PHE B 372
SHEET 4 AB9 4 GLN B 393 LEU B 397 -1 O LEU B 394 N LEU B 386
SHEET 1 AC1 4 ALA B 404 ALA B 408 0
SHEET 2 AC1 4 HIS B 415 GLY B 422 -1 O PHE B 417 N ALA B 408
SHEET 3 AC1 4 THR B 425 ASP B 433 -1 O ALA B 430 N LEU B 418
SHEET 4 AC1 4 PHE B 442 THR B 447 -1 O SER B 443 N ARG B 431
SHEET 1 AC2 8 PHE B 458 GLU B 466 0
SHEET 2 AC2 8 LYS B 472 HIS B 480 -1 O ILE B 473 N TYR B 465
SHEET 3 AC2 8 ILE B 521 PRO B 525 -1 O PHE B 522 N VAL B 478
SHEET 4 AC2 8 ALA B 491 TYR B 494 1 N ILE B 492 O ILE B 521
SHEET 5 AC2 8 VAL B 571 ALA B 576 1 O ALA B 572 N GLN B 493
SHEET 6 AC2 8 ALA B 597 GLU B 601 1 O GLU B 601 N GLY B 575
SHEET 7 AC2 8 ALA B 652 ASN B 658 1 O LEU B 654 N ALA B 598
SHEET 8 AC2 8 LEU B 687 ASP B 692 1 O LYS B 690 N ILE B 655
SHEET 1 AC3 2 VAL C 20 SER C 25 0
SHEET 2 AC3 2 GLY C 29 PRO C 34 -1 O VAL C 33 N ASP C 21
SHEET 1 AC4 3 LYS C 83 PHE C 84 0
SHEET 2 AC4 3 TRP C 95 ASN C 100 -1 O ASN C 100 N LYS C 83
SHEET 3 AC4 3 THR C 88 LEU C 89 -1 N THR C 88 O TYR C 96
SHEET 1 AC5 4 LYS C 83 PHE C 84 0
SHEET 2 AC5 4 TRP C 95 ASN C 100 -1 O ASN C 100 N LYS C 83
SHEET 3 AC5 4 VAL C 108 SER C 112 -1 O TYR C 110 N TRP C 97
SHEET 4 AC5 4 GLY C 128 PHE C 132 -1 O PHE C 131 N LEU C 109
SHEET 1 AC6 4 ALA C 143 PHE C 150 0
SHEET 2 AC6 4 PHE C 156 HIS C 163 -1 O ALA C 160 N LEU C 147
SHEET 3 AC6 4 SER C 169 SER C 175 -1 O THR C 170 N VAL C 161
SHEET 4 AC6 4 VAL C 197 PHE C 200 -1 O VAL C 197 N ILE C 171
SHEET 1 AC7 4 ILE C 206 TRP C 207 0
SHEET 2 AC7 4 GLY C 213 ARG C 218 -1 O LEU C 215 N ILE C 206
SHEET 3 AC7 4 MET C 235 LYS C 240 -1 O HIS C 239 N PHE C 214
SHEET 4 AC7 4 ILE C 249 TYR C 252 -1 O TYR C 252 N MET C 236
SHEET 1 AC8 4 ILE C 261 THR C 266 0
SHEET 2 AC8 4 TYR C 272 PHE C 278 -1 O TYR C 274 N ASP C 265
SHEET 3 AC8 4 LEU C 286 GLU C 291 -1 O ALA C 290 N LEU C 273
SHEET 4 AC8 4 ARG C 304 VAL C 307 -1 O ARG C 304 N VAL C 289
SHEET 1 AC9 4 TYR C 314 HIS C 320 0
SHEET 2 AC9 4 LEU C 323 THR C 328 -1 O TYR C 325 N ILE C 317
SHEET 3 AC9 4 LYS C 336 ASP C 341 -1 O ILE C 338 N ILE C 326
SHEET 4 AC9 4 GLU C 348 ILE C 353 -1 O PHE C 352 N VAL C 337
SHEET 1 AD1 4 LYS C 360 ALA C 367 0
SHEET 2 AD1 4 TYR C 371 ARG C 378 -1 O ILE C 375 N GLN C 363
SHEET 3 AD1 4 LYS C 381 TYR C 387 -1 O TYR C 387 N PHE C 372
SHEET 4 AD1 4 GLN C 393 LEU C 397 -1 O LEU C 394 N LEU C 386
SHEET 1 AD2 4 ALA C 404 ALA C 408 0
SHEET 2 AD2 4 HIS C 415 GLY C 422 -1 O PHE C 417 N ALA C 408
SHEET 3 AD2 4 THR C 425 ASP C 433 -1 O ALA C 430 N LEU C 418
SHEET 4 AD2 4 PHE C 442 THR C 447 -1 O SER C 443 N ARG C 431
SHEET 1 AD3 8 PHE C 458 GLU C 466 0
SHEET 2 AD3 8 LYS C 472 HIS C 480 -1 O ILE C 473 N TYR C 465
SHEET 3 AD3 8 ILE C 521 PRO C 525 -1 O PHE C 522 N VAL C 478
SHEET 4 AD3 8 ALA C 491 TYR C 494 1 N ILE C 492 O ILE C 521
SHEET 5 AD3 8 VAL C 571 ALA C 576 1 O ALA C 572 N GLN C 493
SHEET 6 AD3 8 ALA C 597 GLU C 601 1 O GLU C 601 N GLY C 575
SHEET 7 AD3 8 ALA C 652 ASN C 658 1 O LEU C 654 N ALA C 598
SHEET 8 AD3 8 LEU C 687 ASP C 692 1 O LYS C 690 N ILE C 655
SHEET 1 AD4 2 VAL D 20 SER D 25 0
SHEET 2 AD4 2 GLY D 29 PRO D 34 -1 O VAL D 33 N ASP D 21
SHEET 1 AD5 3 LYS D 83 PHE D 84 0
SHEET 2 AD5 3 TRP D 95 ASN D 100 -1 O ASN D 100 N LYS D 83
SHEET 3 AD5 3 THR D 88 LEU D 89 -1 N THR D 88 O TYR D 96
SHEET 1 AD6 4 LYS D 83 PHE D 84 0
SHEET 2 AD6 4 TRP D 95 ASN D 100 -1 O ASN D 100 N LYS D 83
SHEET 3 AD6 4 VAL D 108 SER D 112 -1 O TYR D 110 N TRP D 97
SHEET 4 AD6 4 GLY D 128 PHE D 132 -1 O PHE D 132 N LEU D 109
SHEET 1 AD7 4 ALA D 143 PHE D 150 0
SHEET 2 AD7 4 PHE D 156 HIS D 163 -1 O ALA D 160 N LEU D 147
SHEET 3 AD7 4 SER D 169 SER D 175 -1 O THR D 170 N VAL D 161
SHEET 4 AD7 4 VAL D 197 PHE D 200 -1 O VAL D 197 N ILE D 171
SHEET 1 AD8 4 ILE D 206 TRP D 207 0
SHEET 2 AD8 4 GLY D 213 ARG D 218 -1 O LEU D 215 N ILE D 206
SHEET 3 AD8 4 MET D 235 LYS D 240 -1 O HIS D 239 N PHE D 214
SHEET 4 AD8 4 ILE D 249 TYR D 252 -1 O VAL D 251 N MET D 236
SHEET 1 AD9 4 ILE D 261 THR D 266 0
SHEET 2 AD9 4 TYR D 272 PHE D 278 -1 O TYR D 274 N ASP D 265
SHEET 3 AD9 4 LEU D 286 GLU D 291 -1 O ALA D 290 N LEU D 273
SHEET 4 AD9 4 ARG D 304 VAL D 307 -1 O VAL D 307 N LEU D 287
SHEET 1 AE1 4 TYR D 314 HIS D 320 0
SHEET 2 AE1 4 LEU D 323 THR D 328 -1 O TYR D 325 N ILE D 317
SHEET 3 AE1 4 LYS D 336 ASP D 341 -1 O ILE D 338 N ILE D 326
SHEET 4 AE1 4 GLU D 348 ILE D 353 -1 O PHE D 352 N VAL D 337
SHEET 1 AE2 4 LYS D 360 ALA D 367 0
SHEET 2 AE2 4 TYR D 371 ARG D 378 -1 O ILE D 375 N GLN D 363
SHEET 3 AE2 4 LYS D 381 TYR D 387 -1 O TYR D 387 N PHE D 372
SHEET 4 AE2 4 GLN D 393 LEU D 397 -1 O LEU D 394 N LEU D 386
SHEET 1 AE3 4 ALA D 404 ALA D 408 0
SHEET 2 AE3 4 HIS D 415 GLY D 422 -1 O PHE D 417 N ALA D 408
SHEET 3 AE3 4 THR D 425 ASP D 433 -1 O ALA D 430 N LEU D 418
SHEET 4 AE3 4 PHE D 442 THR D 447 -1 O SER D 443 N ARG D 431
SHEET 1 AE4 8 PHE D 458 GLU D 466 0
SHEET 2 AE4 8 LYS D 472 HIS D 480 -1 O ILE D 473 N TYR D 465
SHEET 3 AE4 8 ILE D 521 PRO D 525 -1 O PHE D 522 N VAL D 478
SHEET 4 AE4 8 ALA D 491 TYR D 494 1 N ILE D 492 O ILE D 521
SHEET 5 AE4 8 VAL D 571 ALA D 576 1 O ALA D 572 N GLN D 493
SHEET 6 AE4 8 ALA D 597 GLU D 601 1 O GLU D 601 N GLY D 575
SHEET 7 AE4 8 ALA D 652 ASN D 658 1 O LEU D 654 N ALA D 598
SHEET 8 AE4 8 LEU D 687 ASP D 692 1 O LYS D 690 N ILE D 655
SITE 1 AC1 4 ALA D 7 PRO D 8 PRO D 684 PRO D 686
CRYST1 100.797 142.562 116.356 90.00 90.29 90.00 P 1 21 1 8
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 0.009921 0.000000 0.000051 0.00000
SCALE2 0.000000 0.007014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008594 0.00000
TER 5745 LYS A 727
TER 5988 CYS E 35
TER 11720 LEU B 726
TER 17445 THR C 728
TER 23160 LEU D 726
TER 23406 CYS F 35
TER 23657 CYS G 35
TER 23908 CYS H 35
MASTER 990 0 1 93 164 0 1 625078 8 6 240
END |