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HEADER HYDROLASE 08-FEB-12 4DNQ
TITLE CRYSTAL STRUCTURE OF DAD2 S96A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DAD2;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE 3 ORGANISM_TAXID: 4102;
SOURCE 4 GENE: DAD2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST566
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX
REVDAT 1 14-NOV-12 4DNQ 0
JRNL AUTH C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
JRNL AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
JRNL TITL DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE
JRNL TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE
JRNL REF CURR.BIOL. 2012
JRNL REFN ISSN 0960-9822
JRNL PMID 22959345
JRNL DOI 10.1016/J.CUB.2012.08.007
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 92536
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4632
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6554
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 314
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24719
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 0.60000
REMARK 3 B12 (A**2) : -0.20000
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): 0.413
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.322
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.758
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.891
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25337 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34486 ; 1.463 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3141 ; 5.795 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1183 ;27.878 ;22.595
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3926 ;18.336 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 216 ;23.140 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3895 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19504 ; 0.005 ; 0.021
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): 15667 ; 0.329 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25218 ; 0.611 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9670 ; 1.023 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9268 ; 1.509 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 266 2
REMARK 3 1 B 4 B 266 2
REMARK 3 1 C 4 C 266 2
REMARK 3 1 D 4 D 266 2
REMARK 3 1 E 4 E 266 2
REMARK 3 1 F 4 F 266 2
REMARK 3 1 G 4 G 266 2
REMARK 3 1 H 4 H 266 2
REMARK 3 1 I 4 I 266 2
REMARK 3 1 J 4 J 266 2
REMARK 3 1 K 4 K 266 2
REMARK 3 1 L 4 L 266 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 E (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 F (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 G (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 H (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 I (A): 1048 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 J (A): 1048 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 K (A): 1048 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 L (A): 1048 ; 0.050 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1006 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 F (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 G (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 H (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 I (A): 1006 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 J (A): 1006 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 K (A): 1006 ; 0.070 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 L (A): 1006 ; 0.060 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 1048 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 1048 ; 0.120 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 E (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 F (A**2): 1048 ; 0.120 ; 0.500
REMARK 3 TIGHT THERMAL 1 G (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 H (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 I (A**2): 1048 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 J (A**2): 1048 ; 0.090 ; 0.500
REMARK 3 TIGHT THERMAL 1 K (A**2): 1048 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 1 L (A**2): 1048 ; 0.100 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1006 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1006 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1006 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1006 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 1006 ; 0.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 F (A**2): 1006 ; 0.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 G (A**2): 1006 ; 0.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 H (A**2): 1006 ; 0.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 I (A**2): 1006 ; 0.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 J (A**2): 1006 ; 0.110 ; 2.000
REMARK 3 MEDIUM THERMAL 1 K (A**2): 1006 ; 0.110 ; 2.000
REMARK 3 MEDIUM THERMAL 1 L (A**2): 1006 ; 0.110 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 265
REMARK 3 ORIGIN FOR THE GROUP (A): 79.1965 -19.3161 15.3724
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.0304
REMARK 3 T33: 0.1265 T12: 0.0212
REMARK 3 T13: -0.0447 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 2.0128 L22: 5.1863
REMARK 3 L33: 3.5979 L12: 0.7888
REMARK 3 L13: -0.6536 L23: 0.2351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: -0.1664 S13: 0.2920
REMARK 3 S21: 0.3607 S22: 0.0552 S23: 0.1843
REMARK 3 S31: -0.1198 S32: 0.0716 S33: -0.0306
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 265
REMARK 3 ORIGIN FOR THE GROUP (A): 65.7580 26.5285 17.2871
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.2075
REMARK 3 T33: 0.1821 T12: -0.0373
REMARK 3 T13: 0.1034 T23: -0.1014
REMARK 3 L TENSOR
REMARK 3 L11: 4.8425 L22: 3.1995
REMARK 3 L33: 2.8654 L12: 0.5659
REMARK 3 L13: 0.3989 L23: 0.1396
REMARK 3 S TENSOR
REMARK 3 S11: -0.0456 S12: -0.3078 S13: -0.2970
REMARK 3 S21: 0.4250 S22: 0.0831 S23: -0.1156
REMARK 3 S31: -0.0591 S32: -0.2348 S33: -0.0375
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 265
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3243 -9.1012 17.8090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.3281
REMARK 3 T33: 0.1717 T12: 0.0872
REMARK 3 T13: 0.0271 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 3.4696 L22: 3.6420
REMARK 3 L33: 1.9401 L12: -0.4831
REMARK 3 L13: -0.4674 L23: -0.5999
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.0814 S13: -0.1188
REMARK 3 S21: -0.1393 S22: -0.0307 S23: -0.7288
REMARK 3 S31: 0.3003 S32: 0.4966 S33: 0.0658
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 265
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0812 3.4639 -0.5536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0994 T22: 0.2456
REMARK 3 T33: 0.0610 T12: -0.0090
REMARK 3 T13: -0.0330 T23: 0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 3.9852 L22: 3.4550
REMARK 3 L33: 3.3658 L12: 1.1801
REMARK 3 L13: 1.6837 L23: 0.5980
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: 0.2790 S13: 0.4726
REMARK 3 S21: -0.1264 S22: -0.0881 S23: 0.2256
REMARK 3 S31: -0.3050 S32: -0.1405 S33: 0.2253
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 4 E 265
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3978 20.3207 -2.4579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1898 T22: 0.3759
REMARK 3 T33: 0.0918 T12: -0.1258
REMARK 3 T13: -0.0104 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 3.2609 L22: 3.1922
REMARK 3 L33: 3.4213 L12: 0.4906
REMARK 3 L13: 1.0030 L23: -0.9542
REMARK 3 S TENSOR
REMARK 3 S11: -0.1220 S12: 0.5224 S13: -0.2778
REMARK 3 S21: -0.5914 S22: 0.3971 S23: 0.2519
REMARK 3 S31: 0.3672 S32: -0.1537 S33: -0.2751
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 4 F 265
REMARK 3 ORIGIN FOR THE GROUP (A): 93.0169 11.5885 -2.1349
REMARK 3 T TENSOR
REMARK 3 T11: 0.1039 T22: 0.1712
REMARK 3 T33: 0.2241 T12: -0.0015
REMARK 3 T13: 0.0412 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 3.1719 L22: 4.8901
REMARK 3 L33: 1.3107 L12: -1.6603
REMARK 3 L13: -0.5718 L23: -0.7388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1297 S12: 0.2351 S13: 0.2786
REMARK 3 S21: -0.2697 S22: -0.2033 S23: -0.3051
REMARK 3 S31: 0.0902 S32: 0.0170 S33: 0.0736
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 4 G 265
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5926 -43.2475 25.4851
REMARK 3 T TENSOR
REMARK 3 T11: 0.2439 T22: 0.1881
REMARK 3 T33: 0.0521 T12: 0.0156
REMARK 3 T13: -0.0423 T23: 0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 2.0039 L22: 3.8303
REMARK 3 L33: 4.9499 L12: -0.1139
REMARK 3 L13: -0.0803 L23: -0.8461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0498 S12: -0.0467 S13: -0.0310
REMARK 3 S21: 0.6171 S22: -0.0548 S23: 0.0517
REMARK 3 S31: -0.0518 S32: -0.2178 S33: 0.0051
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 4 H 265
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9777 50.1882 26.2250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1534 T22: 0.1921
REMARK 3 T33: 0.1141 T12: 0.0405
REMARK 3 T13: 0.0331 T23: -0.0979
REMARK 3 L TENSOR
REMARK 3 L11: 2.2960 L22: 3.9295
REMARK 3 L33: 5.0154 L12: -0.1503
REMARK 3 L13: -0.3716 L23: 0.4422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0869 S13: 0.1865
REMARK 3 S21: -0.0424 S22: 0.0741 S23: -0.2338
REMARK 3 S31: -0.5277 S32: 0.2040 S33: -0.0673
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 4 I 265
REMARK 3 ORIGIN FOR THE GROUP (A): 84.4456 -56.2001 -3.9100
REMARK 3 T TENSOR
REMARK 3 T11: 0.1265 T22: 0.1473
REMARK 3 T33: 0.5648 T12: -0.0001
REMARK 3 T13: 0.1518 T23: -0.2158
REMARK 3 L TENSOR
REMARK 3 L11: 7.1278 L22: 3.6139
REMARK 3 L33: 2.9268 L12: -2.6472
REMARK 3 L13: -1.4035 L23: 0.6849
REMARK 3 S TENSOR
REMARK 3 S11: -0.3499 S12: 0.7780 S13: -1.6056
REMARK 3 S21: 0.0765 S22: -0.1938 S23: 0.7865
REMARK 3 S31: 0.5224 S32: 0.0522 S33: 0.5437
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 4 J 265
REMARK 3 ORIGIN FOR THE GROUP (A): 94.6401 49.8844 -2.7236
REMARK 3 T TENSOR
REMARK 3 T11: 0.2650 T22: 0.1508
REMARK 3 T33: 0.7033 T12: -0.0434
REMARK 3 T13: 0.0768 T23: 0.2394
REMARK 3 L TENSOR
REMARK 3 L11: 1.9978 L22: 8.2753
REMARK 3 L33: 4.2769 L12: -0.8863
REMARK 3 L13: 0.4629 L23: -0.4011
REMARK 3 S TENSOR
REMARK 3 S11: 0.2166 S12: 0.1959 S13: 0.2650
REMARK 3 S21: -0.2875 S22: -0.5131 S23: -1.8956
REMARK 3 S31: -0.8608 S32: 0.3117 S33: 0.2965
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 4 K 265
REMARK 3 ORIGIN FOR THE GROUP (A): 52.2432 -35.5550 -5.0583
REMARK 3 T TENSOR
REMARK 3 T11: 0.0585 T22: 0.5059
REMARK 3 T33: 0.3322 T12: -0.0178
REMARK 3 T13: 0.0574 T23: -0.2128
REMARK 3 L TENSOR
REMARK 3 L11: 7.4675 L22: 3.6277
REMARK 3 L33: 2.7479 L12: -1.6293
REMARK 3 L13: -1.0030 L23: 0.3095
REMARK 3 S TENSOR
REMARK 3 S11: 0.2313 S12: 0.9000 S13: 0.5637
REMARK 3 S21: -0.3005 S22: -0.0616 S23: -0.3008
REMARK 3 S31: -0.2102 S32: 0.1520 S33: -0.1697
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 4 L 265
REMARK 3 ORIGIN FOR THE GROUP (A): 117.9757 -7.0308 26.0309
REMARK 3 T TENSOR
REMARK 3 T11: 0.3695 T22: 0.5030
REMARK 3 T33: 0.2338 T12: 0.1116
REMARK 3 T13: 0.0189 T23: 0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 2.1157 L22: 2.6841
REMARK 3 L33: 4.2326 L12: 0.6624
REMARK 3 L13: 0.0173 L23: -0.1382
REMARK 3 S TENSOR
REMARK 3 S11: 0.1928 S12: -0.1693 S13: -0.2815
REMARK 3 S21: 0.2339 S22: -0.2398 S23: -0.1799
REMARK 3 S31: 0.4620 S32: 0.0429 S33: 0.0470
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4DNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92560
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 62.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.100
REMARK 200 R MERGE (I) : 0.18200
REMARK 200 R SYM (I) : 0.18200
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : 0.53000
REMARK 200 FOR SHELL : 4.500
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 (%): 54.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2HPO4 0.2M, PEG 3350 18%, PH 6.6,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 35.89000
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 71.78000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 266
REMARK 465 ARG A 267
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 266
REMARK 465 ARG B 267
REMARK 465 GLY C -1
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 HIS C 266
REMARK 465 ARG C 267
REMARK 465 GLY D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 HIS D 266
REMARK 465 ARG D 267
REMARK 465 GLY E -1
REMARK 465 GLY E 0
REMARK 465 MET E 1
REMARK 465 GLY E 2
REMARK 465 GLN E 3
REMARK 465 HIS E 266
REMARK 465 ARG E 267
REMARK 465 GLY F -1
REMARK 465 GLY F 0
REMARK 465 MET F 1
REMARK 465 GLY F 2
REMARK 465 HIS F 266
REMARK 465 ARG F 267
REMARK 465 GLY G -1
REMARK 465 GLY G 0
REMARK 465 MET G 1
REMARK 465 GLY G 2
REMARK 465 HIS G 266
REMARK 465 ARG G 267
REMARK 465 GLY H -1
REMARK 465 GLY H 0
REMARK 465 MET H 1
REMARK 465 GLY H 2
REMARK 465 GLN H 3
REMARK 465 HIS H 266
REMARK 465 ARG H 267
REMARK 465 GLY I -1
REMARK 465 GLY I 0
REMARK 465 MET I 1
REMARK 465 HIS I 266
REMARK 465 ARG I 267
REMARK 465 GLY J -1
REMARK 465 GLY J 0
REMARK 465 MET J 1
REMARK 465 GLY J 2
REMARK 465 HIS J 266
REMARK 465 ARG J 267
REMARK 465 GLY K -1
REMARK 465 GLY K 0
REMARK 465 MET K 1
REMARK 465 GLY K 2
REMARK 465 GLN K 3
REMARK 465 HIS K 266
REMARK 465 ARG K 267
REMARK 465 GLY L -1
REMARK 465 GLY L 0
REMARK 465 MET L 1
REMARK 465 HIS L 266
REMARK 465 ARG L 267
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 OD2 ASP F 88 CD ARG L 19 2.06
REMARK 500 NH1 ARG C 12 O HOH C 311 2.08
REMARK 500 OE2 GLU H 173 O HOH H 312 2.18
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 OG1 THR I 254 OD2 ASP I 72 3654 1.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 54 CB CYS A 54 SG -0.126
REMARK 500 CYS A 89 CB CYS A 89 SG -0.184
REMARK 500 CYS G 89 CB CYS G 89 SG -0.113
REMARK 500 CYS H 89 CB CYS H 89 SG -0.098
REMARK 500 CYS K 89 CB CYS K 89 SG -0.208
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 A 89 CA - CB - SG ANGL. DEV. = 10.2 DEGREES
REMARK 500 CYS B 89 CA - CB - SG ANGL. DEV. = 18.6 DEGREES
REMARK 500 ARG C 109 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 CYS D 89 CA - CB - SG ANGL. DEV. = 14.8 DEGREES
REMARK 500 CYS F 89 CA - CB - SG ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG G 43 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 CYS H 89 CA - CB - SG ANGL. DEV. = 13.3 DEGREES
REMARK 500 CYS J 89 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 CYS K 89 CB - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 CYS K 89 CA - CB - SG ANGL. DEV. = 21.4 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 A 96 -119.19 45.82
REMARK 500 ASP A 184 -66.41 -20.02
REMARK 500 ARG A 216 58.55 35.28
REMARK 500 THR B 29 -167.61 -120.75
REMARK 500 ALA B 96 -118.44 45.87
REMARK 500 ARG B 124 119.76 -173.51
REMARK 500 ASP B 184 -69.16 -20.75
REMARK 500 ARG B 216 55.27 34.74
REMARK 500 ALA B 252 57.98 -146.77
REMARK 500 LEU B 264 20.18 -76.93
REMARK 500 ALA C 96 -117.85 46.15
REMARK 500 GLU C 129 -61.06 -23.42
REMARK 500 ASP C 184 -68.17 -20.58
REMARK 500 THR D 29 -168.10 -113.20
REMARK 500 ALA D 96 -117.94 46.21
REMARK 500 ASP D 184 -67.18 -20.63
REMARK 500 ARG D 216 56.39 36.88
REMARK 500 ALA E 96 -114.80 50.23
REMARK 500 GLU E 129 -58.75 -28.92
REMARK 500 ASP E 184 -65.65 -20.42
REMARK 500 ARG E 216 56.06 38.01
REMARK 500 ALA F 96 -117.91 49.50
REMARK 500 ARG F 124 121.17 -171.75
REMARK 500 GLU F 129 -59.36 -27.42
REMARK 500 ASP F 184 -70.47 -22.67
REMARK 500 THR G 29 -166.56 -114.08
REMARK 500 ALA G 96 -121.36 46.04
REMARK 500 LYS G 115 137.65 -170.91
REMARK 500 ASP G 184 -66.44 -19.29
REMARK 500 THR H 29 -169.41 -118.68
REMARK 500 ALA H 96 -121.54 47.80
REMARK 500 ARG H 124 122.19 -173.14
REMARK 500 ASP H 184 -67.02 -21.20
REMARK 500 GLN I 3 -108.36 111.81
REMARK 500 ALA I 96 -118.27 51.89
REMARK 500 ARG I 124 120.31 -170.35
REMARK 500 ASP I 184 -69.61 -17.10
REMARK 500 ALA J 96 -119.78 48.64
REMARK 500 ASP J 184 -68.84 -20.53
REMARK 500 ALA K 96 -120.96 45.33
REMARK 500 ASP K 184 -66.96 -21.18
REMARK 500 ALA L 96 -121.20 47.78
REMARK 500 LYS L 115 136.45 -171.93
REMARK 500 ASP L 184 -68.67 -20.75
REMARK 500 ARG L 216 58.23 35.73
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 F 325 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH K 322 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH L 311 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH L 330 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH L 331 DISTANCE = 5.84 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DNP RELATED DB: PDB
REMARK 900 WILD-TYPE DAD2
DBREF 4DNQ A -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ B -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ C -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ D -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ E -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ F -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ G -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ H -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ I -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ J -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ K -1 267 PDB 4DNQ 4DNQ -1 267
DBREF 4DNQ L -1 267 PDB 4DNQ 4DNQ -1 267
SEQRES 1 A 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 A 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 A 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 A 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 A 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 A 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 A 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 A 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 A 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 A 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 A 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 A 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 A 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 A 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 A 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 A 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 A 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 A 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 A 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 A 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 B 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 B 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 B 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 B 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 B 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 B 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 B 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 B 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 B 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 B 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 B 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 B 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 B 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 B 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 B 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 B 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 B 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 B 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 B 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 B 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 B 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 C 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 C 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 C 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 C 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 C 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 C 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 C 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 C 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 C 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 C 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 C 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 C 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 C 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 C 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 C 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 C 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 C 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 C 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 C 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 C 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 C 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 D 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 D 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 D 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 D 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 D 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 D 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 D 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 D 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 D 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 D 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 D 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 D 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 D 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 D 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 D 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 D 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 D 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 D 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 D 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 D 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 D 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 E 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 E 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 E 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 E 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 E 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 E 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 E 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 E 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 E 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 E 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 E 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 E 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 E 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 E 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 E 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 E 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 E 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 E 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 E 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 E 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 E 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 F 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 F 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 F 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 F 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 F 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 F 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 F 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 F 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 F 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 F 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 F 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 F 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 F 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 F 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 F 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 F 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 F 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 F 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 F 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 F 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 F 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 G 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 G 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 G 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 G 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 G 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 G 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 G 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 G 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 G 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 G 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 G 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 G 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 G 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 G 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 G 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 G 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 G 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 G 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 G 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 G 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 G 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 H 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 H 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 H 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 H 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 H 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 H 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 H 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 H 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 H 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 H 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 H 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 H 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 H 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 H 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 H 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 H 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 H 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 H 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 H 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 H 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 H 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 I 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 I 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 I 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 I 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 I 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 I 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 I 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 I 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 I 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 I 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 I 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 I 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 I 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 I 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 I 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 I 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 I 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 I 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 I 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 I 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 I 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 J 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 J 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 J 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 J 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 J 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 J 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 J 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 J 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 J 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 J 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 J 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 J 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 J 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 J 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 J 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 J 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 J 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 J 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 J 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 J 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 J 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 K 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 K 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 K 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 K 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 K 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 K 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 K 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 K 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 K 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 K 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 K 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 K 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 K 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 K 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 K 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 K 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 K 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 K 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 K 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 K 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 K 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 L 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 L 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 L 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 L 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 L 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 L 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 L 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP CYS
SEQRES 8 L 269 CYS ALA TYR VAL GLY HIS ALA VAL SER ALA MET ILE GLY
SEQRES 9 L 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 L 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 L 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 L 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 L 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 L 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 L 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 L 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 L 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 L 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 L 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES 20 L 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 L 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
FORMUL 13 HOH *323(H2 O)
HELIX 1 1 THR A 4 LEU A 9 1 6
HELIX 2 2 ASP A 30 ASN A 35 5 6
HELIX 3 3 ILE A 37 PHE A 41 5 5
HELIX 4 4 ASN A 59 PHE A 63 5 5
HELIX 5 5 LEU A 71 LEU A 85 1 15
HELIX 6 6 ALA A 96 ARG A 109 1 14
HELIX 7 7 GLU A 136 ASN A 150 1 15
HELIX 8 8 ASN A 150 GLY A 164 1 15
HELIX 9 9 VAL A 167 MET A 181 1 15
HELIX 10 10 ARG A 182 ASN A 195 1 14
HELIX 11 11 MET A 198 VAL A 205 5 8
HELIX 12 12 PRO A 221 LEU A 232 1 12
HELIX 13 13 LEU A 247 ALA A 252 1 6
HELIX 14 14 ALA A 252 LEU A 264 1 13
HELIX 15 15 LEU B 5 LEU B 9 1 5
HELIX 16 16 ASP B 30 ASN B 35 5 6
HELIX 17 17 ILE B 37 PHE B 41 5 5
HELIX 18 18 ASN B 59 PHE B 63 5 5
HELIX 19 19 LEU B 71 LEU B 85 1 15
HELIX 20 20 ALA B 96 ARG B 109 1 14
HELIX 21 21 GLU B 136 ASN B 150 1 15
HELIX 22 22 ASN B 150 GLY B 164 1 15
HELIX 23 23 VAL B 167 MET B 181 1 15
HELIX 24 24 ARG B 182 ASN B 195 1 14
HELIX 25 25 MET B 198 VAL B 205 5 8
HELIX 26 26 PRO B 221 LEU B 232 1 12
HELIX 27 27 LEU B 247 ALA B 252 1 6
HELIX 28 28 ALA B 252 LEU B 264 1 13
HELIX 29 29 THR C 4 LEU C 9 1 6
HELIX 30 30 ASP C 30 ASN C 35 5 6
HELIX 31 31 ILE C 37 PHE C 41 5 5
HELIX 32 32 ASN C 59 PHE C 63 5 5
HELIX 33 33 LEU C 71 LEU C 85 1 15
HELIX 34 34 ALA C 96 ARG C 109 1 14
HELIX 35 35 GLU C 136 ASN C 150 1 15
HELIX 36 36 ASN C 150 GLY C 164 1 15
HELIX 37 37 VAL C 167 ASN C 180 1 14
HELIX 38 38 ARG C 182 ASN C 195 1 14
HELIX 39 39 MET C 198 VAL C 205 5 8
HELIX 40 40 PRO C 221 LEU C 232 1 12
HELIX 41 41 LEU C 247 ALA C 252 1 6
HELIX 42 42 ALA C 252 LEU C 264 1 13
HELIX 43 43 THR D 4 LEU D 9 1 6
HELIX 44 44 ASP D 30 ASN D 35 5 6
HELIX 45 45 ILE D 37 PHE D 41 5 5
HELIX 46 46 ASN D 59 PHE D 63 5 5
HELIX 47 47 LEU D 71 LEU D 85 1 15
HELIX 48 48 ALA D 96 ARG D 109 1 14
HELIX 49 49 GLU D 136 ASN D 150 1 15
HELIX 50 50 ASN D 150 GLY D 164 1 15
HELIX 51 51 VAL D 167 MET D 181 1 15
HELIX 52 52 ARG D 182 ASN D 195 1 14
HELIX 53 53 MET D 198 VAL D 205 5 8
HELIX 54 54 PRO D 221 LEU D 232 1 12
HELIX 55 55 LEU D 247 ALA D 252 1 6
HELIX 56 56 ALA D 252 LEU D 264 1 13
HELIX 57 57 LEU E 5 LEU E 9 1 5
HELIX 58 58 ASP E 30 ASN E 35 5 6
HELIX 59 59 ILE E 37 PHE E 41 5 5
HELIX 60 60 ASN E 59 PHE E 63 5 5
HELIX 61 61 LEU E 71 LEU E 85 1 15
HELIX 62 62 ALA E 96 ARG E 109 1 14
HELIX 63 63 GLU E 136 ASN E 150 1 15
HELIX 64 64 ASN E 150 GLY E 164 1 15
HELIX 65 65 VAL E 167 MET E 181 1 15
HELIX 66 66 ARG E 182 ASN E 195 1 14
HELIX 67 67 MET E 198 VAL E 205 5 8
HELIX 68 68 PRO E 221 LEU E 232 1 12
HELIX 69 69 LEU E 247 ALA E 252 1 6
HELIX 70 70 ALA E 252 LEU E 264 1 13
HELIX 71 71 THR F 4 LEU F 9 1 6
HELIX 72 72 ASP F 30 ASN F 35 5 6
HELIX 73 73 ILE F 37 PHE F 41 5 5
HELIX 74 74 ASN F 59 PHE F 63 5 5
HELIX 75 75 LEU F 71 LEU F 85 1 15
HELIX 76 76 ALA F 96 ARG F 109 1 14
HELIX 77 77 GLU F 136 ASN F 150 1 15
HELIX 78 78 ASN F 150 GLY F 164 1 15
HELIX 79 79 VAL F 167 MET F 181 1 15
HELIX 80 80 ARG F 182 ASN F 195 1 14
HELIX 81 81 VAL F 201 VAL F 205 5 5
HELIX 82 82 PRO F 221 LEU F 232 1 12
HELIX 83 83 LEU F 247 ALA F 252 1 6
HELIX 84 84 ALA F 252 LEU F 264 1 13
HELIX 85 85 THR G 4 LEU G 9 1 6
HELIX 86 86 ASP G 30 ASN G 35 5 6
HELIX 87 87 ILE G 37 PHE G 41 5 5
HELIX 88 88 ASN G 59 PHE G 63 5 5
HELIX 89 89 LEU G 71 LEU G 85 1 15
HELIX 90 90 ALA G 96 ARG G 109 1 14
HELIX 91 91 GLU G 136 ASN G 150 1 15
HELIX 92 92 ASN G 150 GLY G 164 1 15
HELIX 93 93 VAL G 167 MET G 181 1 15
HELIX 94 94 ARG G 182 ASN G 195 1 14
HELIX 95 95 VAL G 201 VAL G 205 5 5
HELIX 96 96 PRO G 221 LEU G 232 1 12
HELIX 97 97 LEU G 247 ALA G 252 1 6
HELIX 98 98 ALA G 252 LEU G 264 1 13
HELIX 99 99 LEU H 5 LEU H 9 1 5
HELIX 100 100 ASP H 30 ASN H 35 5 6
HELIX 101 101 ILE H 37 PHE H 41 5 5
HELIX 102 102 ASN H 59 PHE H 63 5 5
HELIX 103 103 LEU H 71 LEU H 85 1 15
HELIX 104 104 ALA H 96 ARG H 109 1 14
HELIX 105 105 GLU H 136 ASN H 150 1 15
HELIX 106 106 ASN H 150 GLY H 164 1 15
HELIX 107 107 VAL H 167 MET H 181 1 15
HELIX 108 108 ARG H 182 ASN H 195 1 14
HELIX 109 109 MET H 198 VAL H 205 5 8
HELIX 110 110 PRO H 221 LEU H 232 1 12
HELIX 111 111 LEU H 247 ALA H 252 1 6
HELIX 112 112 ALA H 252 LEU H 264 1 13
HELIX 113 113 GLN I 3 LEU I 9 1 7
HELIX 114 114 ASP I 30 ASN I 35 5 6
HELIX 115 115 ILE I 37 PHE I 41 5 5
HELIX 116 116 ASN I 59 PHE I 63 5 5
HELIX 117 117 LEU I 71 LEU I 85 1 15
HELIX 118 118 ALA I 96 ARG I 109 1 14
HELIX 119 119 GLU I 136 ASN I 150 1 15
HELIX 120 120 ASN I 150 GLY I 164 1 15
HELIX 121 121 VAL I 167 MET I 181 1 15
HELIX 122 122 ARG I 182 ASN I 195 1 14
HELIX 123 123 MET I 198 VAL I 205 5 8
HELIX 124 124 PRO I 221 LEU I 232 1 12
HELIX 125 125 LEU I 247 ALA I 252 1 6
HELIX 126 126 ALA I 252 LEU I 264 1 13
HELIX 127 127 THR J 4 LEU J 9 1 6
HELIX 128 128 ASP J 30 ASN J 35 5 6
HELIX 129 129 ILE J 37 PHE J 41 5 5
HELIX 130 130 ASN J 59 PHE J 63 5 5
HELIX 131 131 LEU J 71 LEU J 85 1 15
HELIX 132 132 ALA J 96 ARG J 109 1 14
HELIX 133 133 GLU J 136 ASN J 150 1 15
HELIX 134 134 ASN J 150 GLY J 164 1 15
HELIX 135 135 VAL J 167 MET J 181 1 15
HELIX 136 136 ARG J 182 ASN J 195 1 14
HELIX 137 137 VAL J 201 VAL J 205 5 5
HELIX 138 138 PRO J 221 LEU J 232 1 12
HELIX 139 139 LEU J 247 ALA J 252 1 6
HELIX 140 140 ALA J 252 LEU J 264 1 13
HELIX 141 141 LEU K 5 LEU K 9 1 5
HELIX 142 142 ASP K 30 ASN K 35 5 6
HELIX 143 143 ILE K 37 PHE K 41 5 5
HELIX 144 144 ASN K 59 PHE K 63 5 5
HELIX 145 145 LEU K 71 LEU K 85 1 15
HELIX 146 146 ALA K 96 ARG K 109 1 14
HELIX 147 147 GLU K 136 ASN K 150 1 15
HELIX 148 148 ASN K 150 GLY K 164 1 15
HELIX 149 149 VAL K 167 MET K 181 1 15
HELIX 150 150 ARG K 182 ASN K 195 1 14
HELIX 151 151 MET K 198 VAL K 205 5 8
HELIX 152 152 PRO K 221 LEU K 232 1 12
HELIX 153 153 LEU K 247 ALA K 252 1 6
HELIX 154 154 ALA K 252 LEU K 264 1 13
HELIX 155 155 THR L 4 LEU L 9 1 6
HELIX 156 156 ASP L 30 ASN L 35 5 6
HELIX 157 157 ILE L 37 PHE L 41 5 5
HELIX 158 158 ASN L 59 PHE L 63 5 5
HELIX 159 159 LEU L 71 LEU L 85 1 15
HELIX 160 160 ALA L 96 ARG L 109 1 14
HELIX 161 161 GLU L 136 ASN L 150 1 15
HELIX 162 162 ASN L 150 GLY L 164 1 15
HELIX 163 163 VAL L 167 MET L 181 1 15
HELIX 164 164 ARG L 182 ASN L 195 1 14
HELIX 165 165 MET L 198 VAL L 205 5 8
HELIX 166 166 PRO L 221 LEU L 232 1 12
HELIX 167 167 LEU L 247 ALA L 252 1 6
HELIX 168 168 ALA L 252 LEU L 264 1 13
SHEET 1 A 7 ARG A 12 VAL A 14 0
SHEET 2 A 7 TYR A 45 TYR A 50 -1 O VAL A 47 N VAL A 14
SHEET 3 A 7 ARG A 19 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 A 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 A 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 A 7 CYS A 209 ALA A 215 1 O PHE A 212 N LEU A 118
SHEET 7 A 7 ASN A 236 GLU A 244 1 O THR A 237 N ILE A 211
SHEET 1 B 7 ARG B 12 VAL B 14 0
SHEET 2 B 7 TYR B 45 TYR B 50 -1 O VAL B 47 N VAL B 14
SHEET 3 B 7 ARG B 19 ALA B 24 1 N LEU B 21 O VAL B 48
SHEET 4 B 7 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 22
SHEET 5 B 7 PHE B 113 ILE B 119 1 O ILE B 117 N TYR B 92
SHEET 6 B 7 CYS B 209 ALA B 215 1 O PHE B 212 N LEU B 118
SHEET 7 B 7 ASN B 236 GLU B 244 1 O THR B 237 N ILE B 211
SHEET 1 C 7 ARG C 12 VAL C 14 0
SHEET 2 C 7 TYR C 45 TYR C 50 -1 O VAL C 47 N VAL C 14
SHEET 3 C 7 ARG C 19 ALA C 24 1 N LEU C 21 O VAL C 48
SHEET 4 C 7 CYS C 90 HIS C 95 1 O VAL C 93 N VAL C 22
SHEET 5 C 7 PHE C 113 ILE C 119 1 O ILE C 117 N TYR C 92
SHEET 6 C 7 CYS C 209 ALA C 215 1 O PHE C 212 N LEU C 118
SHEET 7 C 7 ASN C 236 GLU C 244 1 O THR C 237 N ILE C 211
SHEET 1 D 7 ARG D 12 VAL D 14 0
SHEET 2 D 7 TYR D 45 TYR D 50 -1 O VAL D 47 N VAL D 14
SHEET 3 D 7 ARG D 19 ALA D 24 1 N LEU D 21 O VAL D 48
SHEET 4 D 7 CYS D 90 HIS D 95 1 O VAL D 93 N VAL D 22
SHEET 5 D 7 PHE D 113 ILE D 119 1 O ILE D 117 N TYR D 92
SHEET 6 D 7 CYS D 209 ALA D 215 1 O PHE D 212 N LEU D 118
SHEET 7 D 7 ASN D 236 GLU D 244 1 O THR D 237 N ILE D 211
SHEET 1 E 7 ARG E 12 VAL E 14 0
SHEET 2 E 7 TYR E 45 TYR E 50 -1 O VAL E 47 N VAL E 14
SHEET 3 E 7 ARG E 19 ALA E 24 1 N LEU E 21 O VAL E 48
SHEET 4 E 7 CYS E 90 HIS E 95 1 O VAL E 93 N VAL E 22
SHEET 5 E 7 PHE E 113 ILE E 119 1 O ILE E 117 N TYR E 92
SHEET 6 E 7 CYS E 209 ALA E 215 1 O PHE E 212 N LEU E 118
SHEET 7 E 7 ASN E 236 GLU E 244 1 O THR E 237 N ILE E 211
SHEET 1 F 7 ARG F 12 VAL F 14 0
SHEET 2 F 7 TYR F 45 TYR F 50 -1 O VAL F 47 N VAL F 14
SHEET 3 F 7 ARG F 19 ALA F 24 1 N LEU F 21 O VAL F 48
SHEET 4 F 7 CYS F 90 HIS F 95 1 O VAL F 93 N VAL F 22
SHEET 5 F 7 PHE F 113 ILE F 119 1 O ILE F 117 N TYR F 92
SHEET 6 F 7 CYS F 209 ALA F 215 1 O PHE F 212 N LEU F 118
SHEET 7 F 7 ASN F 236 GLU F 244 1 O THR F 237 N ILE F 211
SHEET 1 G 7 ARG G 12 VAL G 14 0
SHEET 2 G 7 TYR G 45 TYR G 50 -1 O VAL G 47 N VAL G 14
SHEET 3 G 7 ARG G 19 ALA G 24 1 N LEU G 21 O VAL G 48
SHEET 4 G 7 CYS G 90 HIS G 95 1 O VAL G 93 N VAL G 22
SHEET 5 G 7 PHE G 113 ILE G 119 1 O ILE G 117 N TYR G 92
SHEET 6 G 7 CYS G 209 ALA G 215 1 O PHE G 212 N LEU G 118
SHEET 7 G 7 ASN G 236 GLU G 244 1 O THR G 237 N ILE G 211
SHEET 1 H 7 ARG H 12 VAL H 14 0
SHEET 2 H 7 TYR H 45 TYR H 50 -1 O VAL H 47 N VAL H 14
SHEET 3 H 7 ARG H 19 ALA H 24 1 N LEU H 21 O VAL H 48
SHEET 4 H 7 CYS H 90 HIS H 95 1 O VAL H 93 N VAL H 22
SHEET 5 H 7 PHE H 113 ILE H 119 1 O ILE H 117 N TYR H 92
SHEET 6 H 7 CYS H 209 ALA H 215 1 O PHE H 212 N LEU H 118
SHEET 7 H 7 ASN H 236 GLU H 244 1 O THR H 237 N ILE H 211
SHEET 1 I 7 ARG I 12 VAL I 14 0
SHEET 2 I 7 TYR I 45 TYR I 50 -1 O VAL I 47 N VAL I 14
SHEET 3 I 7 ARG I 19 ALA I 24 1 N LEU I 21 O VAL I 48
SHEET 4 I 7 CYS I 90 HIS I 95 1 O VAL I 93 N VAL I 22
SHEET 5 I 7 PHE I 113 ILE I 119 1 O ILE I 117 N TYR I 92
SHEET 6 I 7 CYS I 209 ALA I 215 1 O PHE I 212 N LEU I 118
SHEET 7 I 7 ASN I 236 GLU I 244 1 O THR I 237 N ILE I 211
SHEET 1 J 7 ARG J 12 VAL J 14 0
SHEET 2 J 7 TYR J 45 TYR J 50 -1 O VAL J 47 N VAL J 14
SHEET 3 J 7 ARG J 19 ALA J 24 1 N LEU J 21 O VAL J 48
SHEET 4 J 7 CYS J 90 HIS J 95 1 O VAL J 93 N VAL J 22
SHEET 5 J 7 PHE J 113 ILE J 119 1 O ILE J 117 N TYR J 92
SHEET 6 J 7 CYS J 209 ALA J 215 1 O PHE J 212 N LEU J 118
SHEET 7 J 7 ASN J 236 GLU J 244 1 O HIS J 239 N ILE J 211
SHEET 1 K 7 ARG K 12 VAL K 14 0
SHEET 2 K 7 TYR K 45 TYR K 50 -1 O VAL K 47 N VAL K 14
SHEET 3 K 7 ARG K 19 ALA K 24 1 N LEU K 21 O VAL K 48
SHEET 4 K 7 CYS K 90 HIS K 95 1 O VAL K 93 N VAL K 22
SHEET 5 K 7 PHE K 113 ILE K 119 1 O ILE K 117 N TYR K 92
SHEET 6 K 7 CYS K 209 ALA K 215 1 O PHE K 212 N LEU K 118
SHEET 7 K 7 ASN K 236 GLU K 244 1 O THR K 237 N ILE K 211
SHEET 1 L 7 ARG L 12 VAL L 14 0
SHEET 2 L 7 TYR L 45 TYR L 50 -1 O VAL L 47 N VAL L 14
SHEET 3 L 7 ARG L 19 ALA L 24 1 N LEU L 21 O VAL L 48
SHEET 4 L 7 CYS L 90 HIS L 95 1 O VAL L 93 N VAL L 22
SHEET 5 L 7 PHE L 113 ILE L 119 1 O ILE L 117 N TYR L 92
SHEET 6 L 7 CYS L 209 ALA L 215 1 O PHE L 212 N LEU L 118
SHEET 7 L 7 ASN L 236 GLU L 244 1 O THR L 237 N ILE L 211
SSBOND 1 CYS A 89 CYS I 89 1555 1555 2.11
SSBOND 2 CYS B 89 CYS J 89 1555 1555 2.07
SSBOND 3 CYS C 89 CYS D 89 1555 1555 2.03
SSBOND 4 CYS E 89 CYS H 89 1555 1555 2.03
SSBOND 5 CYS F 89 CYS L 89 1555 1555 2.08
SSBOND 6 CYS G 89 CYS K 89 1555 1555 2.05
CRYST1 176.660 176.660 107.670 90.00 90.00 120.00 P 31 36
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 0.005661 0.003268 0.000000 0.00000
SCALE2 0.000000 0.006536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009288 0.00000
TER 2055 SER A 265
TER 4110 SER B 265
TER 6174 SER C 265
TER 8238 SER D 265
TER 10293 SER E 265
TER 12357 SER F 265
TER 14421 SER G 265
TER 16476 SER H 265
TER 18544 SER I 265
TER 20608 SER J 265
TER 22663 SER K 265
TER 24731 SER L 265
MASTER 854 0 0 168 84 0 0 625042 12 12 252
END |