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HEADER HYDROLASE 27-JAN-11 3QIT
TITLE THIOESTERASE DOMAIN FROM CURACIN BIOSYNTHETIC PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN (UNP RESIDUES 1929-2211);
COMPND 5 SYNONYM: CURM TE;
COMPND 6 EC: 3.1.2.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYNGBYA MAJUSCULA 19L;
SOURCE 3 ORGANISM_TAXID: 276768;
SOURCE 4 GENE: CURM;
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: PMOCR
KEYWDS THIOESTERASE, ALPHA/BETA HYDROLASE, DECARBOXYLASE, SULFATE
KEYWDS 2 ELIMINATION, TERMINAL ALKENE PRODUCTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.GEHRET,J.L.SMITH
REVDAT 1 09-MAR-11 3QIT 0
JRNL AUTH J.J.GEHRET,L.GU,W.H.GERWICK,P.WIPF,D.H.SHERMAN,J.L.SMITH
JRNL TITL TERMINAL ALKENE FORMATION BY THE THIOESTERASE OF CURACIN A
JRNL TITL 2 BIOSYNTHESIS: STRUCTURE OF A DECARBOXYLATING THIOESTERASE.
JRNL REF J.BIOL.CHEM. 2011
JRNL REFN ESSN 1083-351X
JRNL PMID 21357626
JRNL DOI 10.1074/JBC.M110.214635
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 108718
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5806
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4163
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 47.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE SET COUNT : 233
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8617
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.47000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.456
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9035 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12347 ; 1.268 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1194 ; 5.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 370 ;40.331 ;24.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1587 ;12.306 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;17.492 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1447 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6759 ; 0.006 ; 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): 5707 ; 2.551 ; 3.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9268 ; 3.791 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3328 ; 3.504 ; 3.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3035 ; 5.134 ; 5.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 -1 A 106
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7854 44.2163 42.5338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0084 T22: 0.0188
REMARK 3 T33: 0.0399 T12: -0.0064
REMARK 3 T13: 0.0097 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.5394 L22: 0.7621
REMARK 3 L33: 0.6644 L12: -0.2020
REMARK 3 L13: -0.1284 L23: 0.1366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: 0.0189 S13: -0.0443
REMARK 3 S21: -0.0078 S22: -0.0134 S23: 0.1085
REMARK 3 S31: 0.0400 S32: -0.0932 S33: 0.0277
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 107 A 131
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9143 59.6490 41.4239
REMARK 3 T TENSOR
REMARK 3 T11: 0.0320 T22: 0.0070
REMARK 3 T33: 0.0436 T12: 0.0062
REMARK 3 T13: 0.0036 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 2.6120 L22: 0.7250
REMARK 3 L33: 2.2491 L12: 0.0413
REMARK 3 L13: 1.7011 L23: 0.0832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: 0.1082 S13: 0.1131
REMARK 3 S21: -0.0075 S22: -0.0145 S23: 0.0367
REMARK 3 S31: -0.1861 S32: 0.0375 S33: 0.0538
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 134 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): 59.3023 50.4065 38.3809
REMARK 3 T TENSOR
REMARK 3 T11: 0.0459 T22: 0.1407
REMARK 3 T33: 0.0813 T12: -0.0688
REMARK 3 T13: 0.0240 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.3250 L22: 6.9453
REMARK 3 L33: 3.8957 L12: 2.8943
REMARK 3 L13: -1.9615 L23: -4.2335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: 0.0677 S13: -0.0191
REMARK 3 S21: 0.1355 S22: 0.0019 S23: 0.1437
REMARK 3 S31: -0.2378 S32: 0.1833 S33: -0.0353
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 154 A 220
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5583 42.2115 51.8337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0307 T22: 0.0115
REMARK 3 T33: 0.0272 T12: -0.0032
REMARK 3 T13: -0.0028 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.5440 L22: 1.1532
REMARK 3 L33: 0.5062 L12: -0.2767
REMARK 3 L13: 0.3242 L23: -0.2503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0405 S12: -0.0042 S13: -0.0324
REMARK 3 S21: 0.1142 S22: 0.0298 S23: -0.0948
REMARK 3 S31: -0.0140 S32: -0.0028 S33: 0.0107
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 221 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9049 62.5537 52.3592
REMARK 3 T TENSOR
REMARK 3 T11: 0.0500 T22: 0.0157
REMARK 3 T33: 0.0297 T12: 0.0203
REMARK 3 T13: -0.0093 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4309 L22: 1.4207
REMARK 3 L33: 0.2981 L12: -0.1497
REMARK 3 L13: -0.0833 L23: -0.1078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: -0.0402 S13: 0.0895
REMARK 3 S21: 0.1271 S22: 0.0216 S23: 0.0040
REMARK 3 S31: -0.0931 S32: -0.0264 S33: 0.0137
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 -1 B 130
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2606 46.6757 18.0805
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0484
REMARK 3 T33: 0.0380 T12: 0.0104
REMARK 3 T13: 0.0035 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.7576 L22: 0.7586
REMARK 3 L33: 0.5809 L12: 0.3815
REMARK 3 L13: -0.1978 L23: -0.1584
REMARK 3 S TENSOR
REMARK 3 S11: 0.0543 S12: -0.0264 S13: 0.0022
REMARK 3 S21: 0.0339 S22: -0.0517 S23: -0.0763
REMARK 3 S31: 0.0385 S32: 0.0779 S33: -0.0026
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 131 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0043 58.7306 24.4202
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.0254
REMARK 3 T33: 0.0464 T12: 0.0407
REMARK 3 T13: 0.0043 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.9334 L22: 3.0570
REMARK 3 L33: 0.9172 L12: -0.5639
REMARK 3 L13: -0.6254 L23: 1.5410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0929 S12: -0.0039 S13: -0.0547
REMARK 3 S21: -0.0731 S22: -0.0159 S23: -0.2320
REMARK 3 S31: -0.0724 S32: -0.0073 S33: -0.0770
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 154 B 204
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9047 44.1687 3.9724
REMARK 3 T TENSOR
REMARK 3 T11: 0.0375 T22: 0.0429
REMARK 3 T33: 0.0249 T12: 0.0203
REMARK 3 T13: -0.0282 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.3447 L22: 0.7269
REMARK 3 L33: 1.2264 L12: 0.2435
REMARK 3 L13: 0.2814 L23: -0.5516
REMARK 3 S TENSOR
REMARK 3 S11: 0.0383 S12: 0.0694 S13: -0.0093
REMARK 3 S21: -0.1053 S22: -0.0020 S23: 0.1001
REMARK 3 S31: 0.0531 S32: 0.0891 S33: -0.0363
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 : B 207 B 215
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5067 58.1657 23.9936
REMARK 3 T TENSOR
REMARK 3 T11: 0.6472 T22: 0.1375
REMARK 3 T33: 0.6154 T12: -0.0196
REMARK 3 T13: -0.2098 T23: -0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 48.4866 L22: 9.8699
REMARK 3 L33: 7.9758 L12: 20.9473
REMARK 3 L13: 18.4983 L23: 8.8581
REMARK 3 S TENSOR
REMARK 3 S11: 0.4611 S12: 0.7577 S13: -0.7833
REMARK 3 S21: 0.7407 S22: 0.0351 S23: -0.4409
REMARK 3 S31: 0.7469 S32: 0.0319 S33: -0.4962
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 : B 216 B 283
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5066 64.5132 13.4296
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0262
REMARK 3 T33: 0.0766 T12: -0.0026
REMARK 3 T13: 0.0269 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 1.0325 L22: 2.3958
REMARK 3 L33: 1.3551 L12: 0.6185
REMARK 3 L13: -0.1000 L23: 0.3560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: 0.0287 S13: 0.2257
REMARK 3 S21: -0.0904 S22: 0.0018 S23: 0.0457
REMARK 3 S31: -0.2608 S32: 0.0490 S33: -0.0606
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 -1 C 15
REMARK 3 ORIGIN FOR THE GROUP (A): 81.3702 24.9068 24.6483
REMARK 3 T TENSOR
REMARK 3 T11: 0.1557 T22: 0.0346
REMARK 3 T33: 0.1258 T12: 0.0174
REMARK 3 T13: -0.1227 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 2.1032 L22: 0.4911
REMARK 3 L33: 6.6040 L12: -0.9872
REMARK 3 L13: 2.2907 L23: -0.9470
REMARK 3 S TENSOR
REMARK 3 S11: -0.3643 S12: 0.1580 S13: 0.4225
REMARK 3 S21: 0.1954 S22: -0.0570 S23: -0.1994
REMARK 3 S31: -0.4691 S32: 0.1708 S33: 0.4213
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 16 C 146
REMARK 3 ORIGIN FOR THE GROUP (A): 78.6140 12.3231 25.9396
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: 0.0695
REMARK 3 T33: 0.0632 T12: 0.0364
REMARK 3 T13: -0.0266 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.5274 L22: 0.4777
REMARK 3 L33: 1.2223 L12: -0.6690
REMARK 3 L13: 1.0652 L23: -0.7349
REMARK 3 S TENSOR
REMARK 3 S11: -0.1481 S12: -0.0661 S13: -0.0439
REMARK 3 S21: 0.0706 S22: 0.1006 S23: 0.0098
REMARK 3 S31: -0.1199 S32: -0.1141 S33: 0.0475
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 : C 147 C 203
REMARK 3 ORIGIN FOR THE GROUP (A): 66.9679 22.7475 39.5600
REMARK 3 T TENSOR
REMARK 3 T11: 0.2410 T22: 0.2011
REMARK 3 T33: 0.0677 T12: 0.1987
REMARK 3 T13: -0.0086 T23: -0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 1.3661 L22: 1.3892
REMARK 3 L33: 0.3741 L12: 0.4402
REMARK 3 L13: -0.6661 L23: 0.0313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0460 S12: -0.0809 S13: 0.1545
REMARK 3 S21: 0.3041 S22: 0.0922 S23: 0.1717
REMARK 3 S31: 0.0755 S32: 0.0505 S33: -0.0462
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 : C 204 C 215
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6900 12.1354 28.6437
REMARK 3 T TENSOR
REMARK 3 T11: 0.4756 T22: 0.4612
REMARK 3 T33: 0.2766 T12: -0.1302
REMARK 3 T13: 0.1658 T23: 0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 31.7735 L22: 31.7484
REMARK 3 L33: 47.0457 L12: 11.2958
REMARK 3 L13: 8.9114 L23: 9.9179
REMARK 3 S TENSOR
REMARK 3 S11: 1.3572 S12: -2.0403 S13: 0.3033
REMARK 3 S21: 1.2473 S22: -0.3903 S23: 0.2821
REMARK 3 S31: -0.9314 S32: -0.7620 S33: -0.9669
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 : C 216 C 282
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2973 -2.4481 32.4495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0201 T22: 0.0703
REMARK 3 T33: 0.1233 T12: -0.0117
REMARK 3 T13: -0.0070 T23: 0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 1.1320 L22: 2.9366
REMARK 3 L33: 3.0748 L12: -0.7759
REMARK 3 L13: 1.2792 L23: -0.6090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0545 S12: -0.2522 S13: -0.3067
REMARK 3 S21: 0.0295 S22: 0.1896 S23: 0.2311
REMARK 3 S31: 0.2038 S32: -0.3534 S33: -0.2440
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 -1 D 138
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9207 18.1625 4.0126
REMARK 3 T TENSOR
REMARK 3 T11: 0.0071 T22: 0.0438
REMARK 3 T33: 0.0395 T12: 0.0139
REMARK 3 T13: -0.0059 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.3346 L22: 0.5692
REMARK 3 L33: 0.7267 L12: 0.3479
REMARK 3 L13: 0.1446 L23: 0.1910
REMARK 3 S TENSOR
REMARK 3 S11: 0.0300 S12: 0.0016 S13: -0.0420
REMARK 3 S21: 0.0325 S22: -0.0016 S23: -0.0163
REMARK 3 S31: 0.0006 S32: -0.0566 S33: -0.0284
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 : D 139 D 156
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5194 13.8724 4.0091
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.1887
REMARK 3 T33: 0.1216 T12: 0.0325
REMARK 3 T13: -0.0016 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.9693 L22: 5.8951
REMARK 3 L33: 8.8374 L12: -1.5445
REMARK 3 L13: 2.9223 L23: -4.8159
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: -0.0466 S13: -0.0461
REMARK 3 S21: 0.1295 S22: 0.0521 S23: -0.1091
REMARK 3 S31: 0.3607 S32: -0.1642 S33: -0.1767
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 : D 157 D 194
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0754 23.5629 -13.5386
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0363
REMARK 3 T33: 0.0339 T12: 0.0015
REMARK 3 T13: 0.0287 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.7337 L22: 1.2386
REMARK 3 L33: 1.0432 L12: 0.8862
REMARK 3 L13: -0.5110 L23: 0.4219
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: 0.1035 S13: 0.0289
REMARK 3 S21: -0.1842 S22: 0.0635 S23: -0.1480
REMARK 3 S31: -0.1075 S32: -0.0446 S33: -0.0365
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 : D 195 D 206
REMARK 3 ORIGIN FOR THE GROUP (A): 69.3458 19.5334 -1.3224
REMARK 3 T TENSOR
REMARK 3 T11: 0.0543 T22: 0.0824
REMARK 3 T33: 0.1305 T12: 0.0397
REMARK 3 T13: 0.0134 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 4.1675 L22: 0.6966
REMARK 3 L33: 5.5754 L12: 0.4319
REMARK 3 L13: 0.3887 L23: -1.8567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: -0.0420 S13: -0.4212
REMARK 3 S21: -0.1043 S22: -0.0254 S23: -0.0635
REMARK 3 S31: 0.3159 S32: 0.1117 S33: -0.0114
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 : D 215 D 283
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4224 2.1773 -1.5273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0453 T22: 0.0192
REMARK 3 T33: 0.0549 T12: -0.0132
REMARK 3 T13: -0.0214 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.9418 L22: 1.1140
REMARK 3 L33: 1.1677 L12: 0.0514
REMARK 3 L13: 0.1942 L23: 0.1023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.0040 S13: -0.1894
REMARK 3 S21: -0.0123 S22: 0.0723 S23: -0.0694
REMARK 3 S31: 0.2256 S32: -0.0701 S33: -0.1071
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
REMARK 4
REMARK 4 3QIT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114584
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38400
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG3350, 0.1 M TRIS, 0.2 M SODIUM
REMARK 280 CHLORIDE, 2.5% GLYCEROL, PH 8.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 43.45550
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A -2
REMARK 465 SER A 132
REMARK 465 LYS A 133
REMARK 465 LYS A 134
REMARK 465 SER A 283
REMARK 465 SER B -2
REMARK 465 ARG B 205
REMARK 465 SER B 206
REMARK 465 SER C -2
REMARK 465 LYS C 133
REMARK 465 LYS C 134
REMARK 465 GLU C 135
REMARK 465 SER C 136
REMARK 465 SER C 206
REMARK 465 ILE C 207
REMARK 465 LEU C 208
REMARK 465 GLY C 209
REMARK 465 LEU C 210
REMARK 465 ASN C 211
REMARK 465 ASN C 212
REMARK 465 LEU C 213
REMARK 465 PRO C 214
REMARK 465 GLY C 215
REMARK 465 SER C 283
REMARK 465 SER D -2
REMARK 465 SER D 206
REMARK 465 ILE D 207
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 OE2 GLU D 3 NH1 ARG D 63 2.06
REMARK 500 O HOH B 703 O HOH D 286 2.16
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 LEU A 33 -7.66 75.35
REMARK 500 GLU A 34 -155.17 -91.95
REMARK 500 SER A 100 -116.67 57.75
REMARK 500 ARG A 113 52.85 -119.95
REMARK 500 ASN A 190 136.16 -171.82
REMARK 500 THR A 204 63.52 -102.65
REMARK 500 LEU B 33 -8.45 71.06
REMARK 500 GLU B 34 -153.85 -88.91
REMARK 500 SER B 100 -120.63 55.19
REMARK 500 MET B 254 73.04 -108.29
REMARK 500 ALA B 272 40.82 -140.05
REMARK 500 LEU C 33 -8.59 74.53
REMARK 500 GLU C 34 -150.94 -93.52
REMARK 500 SER C 100 -118.03 57.92
REMARK 500 ARG C 113 53.73 -116.70
REMARK 500 THR C 151 148.50 64.82
REMARK 500 ALA C 272 50.46 -145.98
REMARK 500 LEU D 33 -8.03 73.21
REMARK 500 GLU D 34 -148.36 -92.11
REMARK 500 SER D 100 -116.47 57.03
REMARK 500 LEU D 210 72.91 52.10
REMARK 500 ASN D 211 -158.42 -140.84
REMARK 500 MET D 254 74.75 -103.14
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 B 780 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH A 825 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH D1144 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH D1148 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B1077 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH B1091 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH B1114 DISTANCE = 11.01 ANGSTROMS
REMARK 525 HOH A1171 DISTANCE = 7.60 ANGSTROMS
DBREF 3QIT A 1 283 UNP D0E8E2 D0E8E2_9CYAN 1929 2211
DBREF 3QIT B 1 283 UNP D0E8E2 D0E8E2_9CYAN 1929 2211
DBREF 3QIT C 1 283 UNP D0E8E2 D0E8E2_9CYAN 1929 2211
DBREF 3QIT D 1 283 UNP D0E8E2 D0E8E2_9CYAN 1929 2211
SEQADV 3QIT SER A -2 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ASN A -1 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ALA A 0 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT SER B -2 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ASN B -1 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ALA B 0 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT SER C -2 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ASN C -1 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ALA C 0 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT SER D -2 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ASN D -1 UNP D0E8E2 EXPRESSION TAG
SEQADV 3QIT ALA D 0 UNP D0E8E2 EXPRESSION TAG
SEQRES 1 A 286 SER ASN ALA MET GLU GLU LYS PHE LEU GLU PHE GLY GLY
SEQRES 2 A 286 ASN GLN ILE CYS LEU CYS SER TRP GLY SER PRO GLU HIS
SEQRES 3 A 286 PRO VAL VAL LEU CYS ILE HIS GLY ILE LEU GLU GLN GLY
SEQRES 4 A 286 LEU ALA TRP GLN GLU VAL ALA LEU PRO LEU ALA ALA GLN
SEQRES 5 A 286 GLY TYR ARG VAL VAL ALA PRO ASP LEU PHE GLY HIS GLY
SEQRES 6 A 286 ARG SER SER HIS LEU GLU MET VAL THR SER TYR SER SER
SEQRES 7 A 286 LEU THR PHE LEU ALA GLN ILE ASP ARG VAL ILE GLN GLU
SEQRES 8 A 286 LEU PRO ASP GLN PRO LEU LEU LEU VAL GLY HIS SER MET
SEQRES 9 A 286 GLY ALA MET LEU ALA THR ALA ILE ALA SER VAL ARG PRO
SEQRES 10 A 286 LYS LYS ILE LYS GLU LEU ILE LEU VAL GLU LEU PRO LEU
SEQRES 11 A 286 PRO ALA GLU GLU SER LYS LYS GLU SER ALA VAL ASN GLN
SEQRES 12 A 286 LEU THR THR CYS LEU ASP TYR LEU SER SER THR PRO GLN
SEQRES 13 A 286 HIS PRO ILE PHE PRO ASP VAL ALA THR ALA ALA SER ARG
SEQRES 14 A 286 LEU ARG GLN ALA ILE PRO SER LEU SER GLU GLU PHE SER
SEQRES 15 A 286 TYR ILE LEU ALA GLN ARG ILE THR GLN PRO ASN GLN GLY
SEQRES 16 A 286 GLY VAL ARG TRP SER TRP ASP ALA ILE ILE ARG THR ARG
SEQRES 17 A 286 SER ILE LEU GLY LEU ASN ASN LEU PRO GLY GLY ARG SER
SEQRES 18 A 286 GLN TYR LEU GLU MET LEU LYS SER ILE GLN VAL PRO THR
SEQRES 19 A 286 THR LEU VAL TYR GLY ASP SER SER LYS LEU ASN ARG PRO
SEQRES 20 A 286 GLU ASP LEU GLN GLN GLN LYS MET THR MET THR GLN ALA
SEQRES 21 A 286 LYS ARG VAL PHE LEU SER GLY GLY HIS ASN LEU HIS ILE
SEQRES 22 A 286 ASP ALA ALA ALA ALA LEU ALA SER LEU ILE LEU THR SER
SEQRES 1 B 286 SER ASN ALA MET GLU GLU LYS PHE LEU GLU PHE GLY GLY
SEQRES 2 B 286 ASN GLN ILE CYS LEU CYS SER TRP GLY SER PRO GLU HIS
SEQRES 3 B 286 PRO VAL VAL LEU CYS ILE HIS GLY ILE LEU GLU GLN GLY
SEQRES 4 B 286 LEU ALA TRP GLN GLU VAL ALA LEU PRO LEU ALA ALA GLN
SEQRES 5 B 286 GLY TYR ARG VAL VAL ALA PRO ASP LEU PHE GLY HIS GLY
SEQRES 6 B 286 ARG SER SER HIS LEU GLU MET VAL THR SER TYR SER SER
SEQRES 7 B 286 LEU THR PHE LEU ALA GLN ILE ASP ARG VAL ILE GLN GLU
SEQRES 8 B 286 LEU PRO ASP GLN PRO LEU LEU LEU VAL GLY HIS SER MET
SEQRES 9 B 286 GLY ALA MET LEU ALA THR ALA ILE ALA SER VAL ARG PRO
SEQRES 10 B 286 LYS LYS ILE LYS GLU LEU ILE LEU VAL GLU LEU PRO LEU
SEQRES 11 B 286 PRO ALA GLU GLU SER LYS LYS GLU SER ALA VAL ASN GLN
SEQRES 12 B 286 LEU THR THR CYS LEU ASP TYR LEU SER SER THR PRO GLN
SEQRES 13 B 286 HIS PRO ILE PHE PRO ASP VAL ALA THR ALA ALA SER ARG
SEQRES 14 B 286 LEU ARG GLN ALA ILE PRO SER LEU SER GLU GLU PHE SER
SEQRES 15 B 286 TYR ILE LEU ALA GLN ARG ILE THR GLN PRO ASN GLN GLY
SEQRES 16 B 286 GLY VAL ARG TRP SER TRP ASP ALA ILE ILE ARG THR ARG
SEQRES 17 B 286 SER ILE LEU GLY LEU ASN ASN LEU PRO GLY GLY ARG SER
SEQRES 18 B 286 GLN TYR LEU GLU MET LEU LYS SER ILE GLN VAL PRO THR
SEQRES 19 B 286 THR LEU VAL TYR GLY ASP SER SER LYS LEU ASN ARG PRO
SEQRES 20 B 286 GLU ASP LEU GLN GLN GLN LYS MET THR MET THR GLN ALA
SEQRES 21 B 286 LYS ARG VAL PHE LEU SER GLY GLY HIS ASN LEU HIS ILE
SEQRES 22 B 286 ASP ALA ALA ALA ALA LEU ALA SER LEU ILE LEU THR SER
SEQRES 1 C 286 SER ASN ALA MET GLU GLU LYS PHE LEU GLU PHE GLY GLY
SEQRES 2 C 286 ASN GLN ILE CYS LEU CYS SER TRP GLY SER PRO GLU HIS
SEQRES 3 C 286 PRO VAL VAL LEU CYS ILE HIS GLY ILE LEU GLU GLN GLY
SEQRES 4 C 286 LEU ALA TRP GLN GLU VAL ALA LEU PRO LEU ALA ALA GLN
SEQRES 5 C 286 GLY TYR ARG VAL VAL ALA PRO ASP LEU PHE GLY HIS GLY
SEQRES 6 C 286 ARG SER SER HIS LEU GLU MET VAL THR SER TYR SER SER
SEQRES 7 C 286 LEU THR PHE LEU ALA GLN ILE ASP ARG VAL ILE GLN GLU
SEQRES 8 C 286 LEU PRO ASP GLN PRO LEU LEU LEU VAL GLY HIS SER MET
SEQRES 9 C 286 GLY ALA MET LEU ALA THR ALA ILE ALA SER VAL ARG PRO
SEQRES 10 C 286 LYS LYS ILE LYS GLU LEU ILE LEU VAL GLU LEU PRO LEU
SEQRES 11 C 286 PRO ALA GLU GLU SER LYS LYS GLU SER ALA VAL ASN GLN
SEQRES 12 C 286 LEU THR THR CYS LEU ASP TYR LEU SER SER THR PRO GLN
SEQRES 13 C 286 HIS PRO ILE PHE PRO ASP VAL ALA THR ALA ALA SER ARG
SEQRES 14 C 286 LEU ARG GLN ALA ILE PRO SER LEU SER GLU GLU PHE SER
SEQRES 15 C 286 TYR ILE LEU ALA GLN ARG ILE THR GLN PRO ASN GLN GLY
SEQRES 16 C 286 GLY VAL ARG TRP SER TRP ASP ALA ILE ILE ARG THR ARG
SEQRES 17 C 286 SER ILE LEU GLY LEU ASN ASN LEU PRO GLY GLY ARG SER
SEQRES 18 C 286 GLN TYR LEU GLU MET LEU LYS SER ILE GLN VAL PRO THR
SEQRES 19 C 286 THR LEU VAL TYR GLY ASP SER SER LYS LEU ASN ARG PRO
SEQRES 20 C 286 GLU ASP LEU GLN GLN GLN LYS MET THR MET THR GLN ALA
SEQRES 21 C 286 LYS ARG VAL PHE LEU SER GLY GLY HIS ASN LEU HIS ILE
SEQRES 22 C 286 ASP ALA ALA ALA ALA LEU ALA SER LEU ILE LEU THR SER
SEQRES 1 D 286 SER ASN ALA MET GLU GLU LYS PHE LEU GLU PHE GLY GLY
SEQRES 2 D 286 ASN GLN ILE CYS LEU CYS SER TRP GLY SER PRO GLU HIS
SEQRES 3 D 286 PRO VAL VAL LEU CYS ILE HIS GLY ILE LEU GLU GLN GLY
SEQRES 4 D 286 LEU ALA TRP GLN GLU VAL ALA LEU PRO LEU ALA ALA GLN
SEQRES 5 D 286 GLY TYR ARG VAL VAL ALA PRO ASP LEU PHE GLY HIS GLY
SEQRES 6 D 286 ARG SER SER HIS LEU GLU MET VAL THR SER TYR SER SER
SEQRES 7 D 286 LEU THR PHE LEU ALA GLN ILE ASP ARG VAL ILE GLN GLU
SEQRES 8 D 286 LEU PRO ASP GLN PRO LEU LEU LEU VAL GLY HIS SER MET
SEQRES 9 D 286 GLY ALA MET LEU ALA THR ALA ILE ALA SER VAL ARG PRO
SEQRES 10 D 286 LYS LYS ILE LYS GLU LEU ILE LEU VAL GLU LEU PRO LEU
SEQRES 11 D 286 PRO ALA GLU GLU SER LYS LYS GLU SER ALA VAL ASN GLN
SEQRES 12 D 286 LEU THR THR CYS LEU ASP TYR LEU SER SER THR PRO GLN
SEQRES 13 D 286 HIS PRO ILE PHE PRO ASP VAL ALA THR ALA ALA SER ARG
SEQRES 14 D 286 LEU ARG GLN ALA ILE PRO SER LEU SER GLU GLU PHE SER
SEQRES 15 D 286 TYR ILE LEU ALA GLN ARG ILE THR GLN PRO ASN GLN GLY
SEQRES 16 D 286 GLY VAL ARG TRP SER TRP ASP ALA ILE ILE ARG THR ARG
SEQRES 17 D 286 SER ILE LEU GLY LEU ASN ASN LEU PRO GLY GLY ARG SER
SEQRES 18 D 286 GLN TYR LEU GLU MET LEU LYS SER ILE GLN VAL PRO THR
SEQRES 19 D 286 THR LEU VAL TYR GLY ASP SER SER LYS LEU ASN ARG PRO
SEQRES 20 D 286 GLU ASP LEU GLN GLN GLN LYS MET THR MET THR GLN ALA
SEQRES 21 D 286 LYS ARG VAL PHE LEU SER GLY GLY HIS ASN LEU HIS ILE
SEQRES 22 D 286 ASP ALA ALA ALA ALA LEU ALA SER LEU ILE LEU THR SER
FORMUL 5 HOH *1203(H2 O)
HELIX 1 1 GLN A 35 ALA A 38 5 4
HELIX 2 2 TRP A 39 GLN A 49 1 11
HELIX 3 3 MET A 69 TYR A 73 5 5
HELIX 4 4 SER A 74 LEU A 89 1 16
HELIX 5 5 SER A 100 ARG A 113 1 14
HELIX 6 6 SER A 136 SER A 149 1 14
HELIX 7 7 ASP A 159 ILE A 171 1 13
HELIX 8 8 SER A 175 ILE A 186 1 12
HELIX 9 9 ASP A 199 ARG A 203 5 5
HELIX 10 10 THR A 204 GLY A 209 1 6
HELIX 11 11 GLY A 215 ILE A 227 1 13
HELIX 12 12 ARG A 243 MET A 254 1 12
HELIX 13 13 ASN A 267 ALA A 272 1 6
HELIX 14 14 ALA A 272 THR A 282 1 11
HELIX 15 15 GLN B 35 ALA B 38 5 4
HELIX 16 16 TRP B 39 GLN B 49 1 11
HELIX 17 17 MET B 69 TYR B 73 5 5
HELIX 18 18 SER B 74 LEU B 89 1 16
HELIX 19 19 SER B 100 ARG B 113 1 14
HELIX 20 20 SER B 136 SER B 149 1 14
HELIX 21 21 ASP B 159 ILE B 171 1 13
HELIX 22 22 SER B 175 ILE B 186 1 12
HELIX 23 23 ASP B 199 ARG B 203 5 5
HELIX 24 24 GLY B 216 ILE B 227 1 12
HELIX 25 25 ARG B 243 MET B 254 1 12
HELIX 26 26 ASN B 267 ALA B 272 1 6
HELIX 27 27 ALA B 272 THR B 282 1 11
HELIX 28 28 GLN C 35 ALA C 38 5 4
HELIX 29 29 TRP C 39 GLN C 49 1 11
HELIX 30 30 MET C 69 TYR C 73 5 5
HELIX 31 31 SER C 74 LEU C 89 1 16
HELIX 32 32 SER C 100 ARG C 113 1 14
HELIX 33 33 ALA C 137 SER C 150 1 14
HELIX 34 34 ASP C 159 ILE C 171 1 13
HELIX 35 35 SER C 175 ILE C 186 1 12
HELIX 36 36 ASP C 199 THR C 204 5 6
HELIX 37 37 GLY C 216 ILE C 227 1 12
HELIX 38 38 ARG C 243 MET C 254 1 12
HELIX 39 39 ASN C 267 ALA C 272 1 6
HELIX 40 40 ALA C 272 LEU C 281 1 10
HELIX 41 41 GLN D 35 ALA D 38 5 4
HELIX 42 42 TRP D 39 GLN D 49 1 11
HELIX 43 43 MET D 69 TYR D 73 5 5
HELIX 44 44 SER D 74 LEU D 89 1 16
HELIX 45 45 SER D 100 ARG D 113 1 14
HELIX 46 46 SER D 136 SER D 149 1 14
HELIX 47 47 ASP D 159 ILE D 171 1 13
HELIX 48 48 SER D 175 ILE D 186 1 12
HELIX 49 49 ASP D 199 THR D 204 5 6
HELIX 50 50 GLY D 216 ILE D 227 1 12
HELIX 51 51 ARG D 243 MET D 254 1 12
HELIX 52 52 ASN D 267 ALA D 272 1 6
HELIX 53 53 ALA D 272 THR D 282 1 11
SHEET 1 A 8 GLU A 2 PHE A 8 0
SHEET 2 A 8 ASN A 11 TRP A 18 -1 O ILE A 13 N LEU A 6
SHEET 3 A 8 ARG A 52 PRO A 56 -1 O ALA A 55 N CYS A 16
SHEET 4 A 8 VAL A 25 ILE A 29 1 N CYS A 28 O VAL A 54
SHEET 5 A 8 LEU A 94 HIS A 99 1 O LEU A 95 N LEU A 27
SHEET 6 A 8 ILE A 117 VAL A 123 1 O VAL A 123 N GLY A 98
SHEET 7 A 8 THR A 231 GLY A 236 1 O VAL A 234 N LEU A 122
SHEET 8 A 8 LYS A 258 LEU A 262 1 O LYS A 258 N LEU A 233
SHEET 1 B 2 THR A 187 ASN A 190 0
SHEET 2 B 2 GLY A 193 TRP A 196 -1 O ARG A 195 N GLN A 188
SHEET 1 C 8 GLU B 2 PHE B 8 0
SHEET 2 C 8 ASN B 11 TRP B 18 -1 O ILE B 13 N LEU B 6
SHEET 3 C 8 ARG B 52 PRO B 56 -1 O ALA B 55 N CYS B 16
SHEET 4 C 8 VAL B 25 ILE B 29 1 N VAL B 26 O VAL B 54
SHEET 5 C 8 LEU B 94 HIS B 99 1 O VAL B 97 N LEU B 27
SHEET 6 C 8 ILE B 117 VAL B 123 1 O ILE B 121 N LEU B 96
SHEET 7 C 8 THR B 231 GLY B 236 1 O VAL B 234 N LEU B 122
SHEET 8 C 8 LYS B 258 LEU B 262 1 O LYS B 258 N LEU B 233
SHEET 1 D 2 THR B 187 ASN B 190 0
SHEET 2 D 2 GLY B 193 TRP B 196 -1 O ARG B 195 N GLN B 188
SHEET 1 E 8 GLU C 2 PHE C 8 0
SHEET 2 E 8 ASN C 11 TRP C 18 -1 O SER C 17 N GLU C 2
SHEET 3 E 8 ARG C 52 PRO C 56 -1 O ALA C 55 N CYS C 16
SHEET 4 E 8 VAL C 25 ILE C 29 1 N VAL C 26 O VAL C 54
SHEET 5 E 8 LEU C 94 HIS C 99 1 O LEU C 95 N LEU C 27
SHEET 6 E 8 ILE C 117 VAL C 123 1 O VAL C 123 N GLY C 98
SHEET 7 E 8 THR C 231 GLY C 236 1 O VAL C 234 N LEU C 122
SHEET 8 E 8 LYS C 258 LEU C 262 1 O LYS C 258 N LEU C 233
SHEET 1 F 2 THR C 187 ASN C 190 0
SHEET 2 F 2 GLY C 193 TRP C 196 -1 O ARG C 195 N GLN C 188
SHEET 1 G 8 GLU D 2 PHE D 8 0
SHEET 2 G 8 ASN D 11 TRP D 18 -1 O LEU D 15 N LYS D 4
SHEET 3 G 8 ARG D 52 PRO D 56 -1 O ALA D 55 N CYS D 16
SHEET 4 G 8 VAL D 25 ILE D 29 1 N CYS D 28 O VAL D 54
SHEET 5 G 8 LEU D 94 HIS D 99 1 O VAL D 97 N LEU D 27
SHEET 6 G 8 ILE D 117 VAL D 123 1 O ILE D 121 N LEU D 96
SHEET 7 G 8 THR D 231 GLY D 236 1 O VAL D 234 N LEU D 122
SHEET 8 G 8 LYS D 258 LEU D 262 1 O LYS D 258 N LEU D 233
SHEET 1 H 2 THR D 187 ASN D 190 0
SHEET 2 H 2 GLY D 193 TRP D 196 -1 O ARG D 195 N GLN D 188
CISPEP 1 LEU D 213 PRO D 214 0 -3.66
CRYST1 74.560 86.911 87.592 90.00 90.77 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 0.013412 0.000000 0.000181 0.00000
SCALE2 0.000000 0.011506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011418 0.00000
TER 2219 THR A 282
TER 4464 SER B 283
TER 6577 THR C 282
TER 8821 SER D 283
MASTER 704 0 0 53 40 0 0 6 9820 4 0 88
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