HEADER HYDROLASE 12-DEC-12 3ZFW
TITLE CRYSTAL STRUCTURE OF THE TPR DOMAIN OF KINESIN LIGHT CHAIN 2 IN
TITLE 2 COMPLEX WITH A TRYPTOPHAN-ACIDIC CARGO PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN LIGHT CHAIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TPR DOMAIN, RESIDUES 218-477;
COMPND 5 SYNONYM: KLC 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2;
COMPND 9 CHAIN: X, Y;
COMPND 10 SYNONYM: PH DOMAIN-CONTAINING FAMILY M MEMBER 2, SALMONELLA-INDUCED
COMPND 11 FILAMENTS A AND KINESIN-INTERACTING PROTEIN, SIFA AND KINESIN-
COMPND 12 INTERACTING PROTEIN;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: MOL ID 1 AND MOL ID 2 ARE EXPRESSED AS A SINGLE
COMPND 15 ENTITY. IT IS UNCLEAR WHICH OF CHAIN A OR B ARE JOINED TO CHAINS X OR
COMPND 16 Y.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
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_VECTOR: PET28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PET28
KEYWDS HYDROLASE, KINESIN-CARGO RECOGNITION, MOTOR PROTEIN, TPR DOMAIN,
KEYWDS 2 SALMONELLA
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PERNIGO,A.LAMPRECHT,R.A.STEINER,M.P.DODDING
REVDAT 3 20-DEC-23 3ZFW 1 REMARK
REVDAT 2 01-MAY-13 3ZFW 1 JRNL
REVDAT 1 03-APR-13 3ZFW 0
JRNL AUTH S.PERNIGO,A.LAMPRECHT,R.A.STEINER,M.P.DODDING
JRNL TITL STRUCTURAL BASIS FOR KINESIN-1:CARGO RECOGNITION.
JRNL REF SCIENCE V. 340 356 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 23519214
JRNL DOI 10.1126/SCIENCE.1234264
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 17030
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 854
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.67
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2683
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2772
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2519
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3128
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.11
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3749
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 95.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 108.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00820
REMARK 3 B22 (A**2) : -9.06970
REMARK 3 B33 (A**2) : 9.06150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.578
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.784
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.327
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.800
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.334
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3813 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5144 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1382 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 111 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 541 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3813 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 487 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4211 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.11
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.36
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 236 -244
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2874 17.3227 50.0863
REMARK 3 T TENSOR
REMARK 3 T11: 0.3632 T22: 0.5415
REMARK 3 T33: -0.3060 T12: 0.0350
REMARK 3 T13: -0.1891 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 0.5507 L22: 0.4941
REMARK 3 L33: 2.9171 L12: 0.7164
REMARK 3 L13: -1.4421 L23: -0.9059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: 0.0599 S13: -0.0303
REMARK 3 S21: 0.0148 S22: -0.0264 S23: 0.2642
REMARK 3 S31: 0.1062 S32: -0.1026 S33: 0.0370
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 245 - 272
REMARK 3 ORIGIN FOR THE GROUP (A): -29.7350 17.3827 53.4302
REMARK 3 T TENSOR
REMARK 3 T11: 0.5213 T22: 0.4068
REMARK 3 T33: -0.5876 T12: 0.0496
REMARK 3 T13: 0.0033 T23: 0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 5.8659 L22: 1.9467
REMARK 3 L33: 11.1992 L12: 3.5852
REMARK 3 L13: 1.4705 L23: 1.9607
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.4237 S13: -0.0085
REMARK 3 S21: -0.2391 S22: 0.2312 S23: -0.0150
REMARK 3 S31: -0.2207 S32: 0.1745 S33: -0.2177
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 273 - 298
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6737 22.0029 61.8485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2316 T22: 0.5124
REMARK 3 T33: -0.4111 T12: 0.1608
REMARK 3 T13: 0.0163 T23: 0.1433
REMARK 3 L TENSOR
REMARK 3 L11: 1.3192 L22: 3.7975
REMARK 3 L33: 10.8119 L12: -4.0857
REMARK 3 L13: 3.0246 L23: -0.6579
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: 0.1465 S13: 0.1594
REMARK 3 S21: -0.4156 S22: 0.1630 S23: 0.0685
REMARK 3 S31: -0.4804 S32: -0.1281 S33: -0.1342
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 299 - 315
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3418 26.6329 68.8142
REMARK 3 T TENSOR
REMARK 3 T11: 0.5578 T22: 0.3336
REMARK 3 T33: -0.3040 T12: 0.2508
REMARK 3 T13: -0.0740 T23: 0.2103
REMARK 3 L TENSOR
REMARK 3 L11: 0.0163 L22: 6.4804
REMARK 3 L33: 6.1492 L12: 1.4922
REMARK 3 L13: 5.6036 L23: -1.1296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: -0.0271 S13: 0.1377
REMARK 3 S21: -0.1290 S22: 0.1218 S23: -0.0961
REMARK 3 S31: -0.1893 S32: -0.1405 S33: -0.1060
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 316 - 360
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0729 19.4641 78.6929
REMARK 3 T TENSOR
REMARK 3 T11: -0.0211 T22: 0.0209
REMARK 3 T33: -0.1883 T12: 0.0576
REMARK 3 T13: -0.0184 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 5.9977 L22: 3.2813
REMARK 3 L33: 13.6941 L12: -5.4581
REMARK 3 L13: -2.5607 L23: -0.9009
REMARK 3 S TENSOR
REMARK 3 S11: -0.1050 S12: 0.8422 S13: 0.0782
REMARK 3 S21: -0.5187 S22: 0.0635 S23: -0.0269
REMARK 3 S31: -0.6638 S32: -0.6511 S33: 0.0414
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESID 361 - 419
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4844 5.1196 92.1601
REMARK 3 T TENSOR
REMARK 3 T11: -0.0850 T22: -0.0964
REMARK 3 T33: 0.0115 T12: 0.0283
REMARK 3 T13: 0.0085 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 5.0575 L22: 5.7196
REMARK 3 L33: 9.3570 L12: -1.4021
REMARK 3 L13: 2.8637 L23: 0.5464
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: -0.3526 S13: -0.7182
REMARK 3 S21: -0.1205 S22: 0.0914 S23: 0.3816
REMARK 3 S31: 1.0424 S32: -0.3037 S33: -0.0643
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESID 420 - 446
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2999 -5.5573 90.3851
REMARK 3 T TENSOR
REMARK 3 T11: 0.4597 T22: 0.2395
REMARK 3 T33: 0.5561 T12: -0.0715
REMARK 3 T13: -0.1730 T23: 0.1175
REMARK 3 L TENSOR
REMARK 3 L11: 0.9195 L22: 6.0730
REMARK 3 L33: 0.2193 L12: -5.5682
REMARK 3 L13: -0.2089 L23: 0.7742
REMARK 3 S TENSOR
REMARK 3 S11: -0.0503 S12: -0.0261 S13: -0.1925
REMARK 3 S21: -0.1140 S22: 0.0268 S23: 0.1131
REMARK 3 S31: 0.1554 S32: -0.0713 S33: 0.0235
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESID 447 - 460
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8050 2.3474 88.3405
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: -0.1642
REMARK 3 T33: 0.0532 T12: 0.0558
REMARK 3 T13: 0.0113 T23: -0.1846
REMARK 3 L TENSOR
REMARK 3 L11: 1.0585 L22: 4.4137
REMARK 3 L33: 2.1627 L12: -2.1512
REMARK 3 L13: -4.4557 L23: -2.5977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: 0.2135 S13: -0.1429
REMARK 3 S21: -0.0708 S22: -0.1676 S23: -0.4933
REMARK 3 S31: -0.1136 S32: 0.3307 S33: 0.1500
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND RESID 461 - 479
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8604 -2.8867 91.4139
REMARK 3 T TENSOR
REMARK 3 T11: -0.0555 T22: -0.2528
REMARK 3 T33: 0.0788 T12: 0.1707
REMARK 3 T13: -0.0682 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 10.6053 L22: 9.2597
REMARK 3 L33: 4.9743 L12: -5.2826
REMARK 3 L13: -5.5530 L23: 1.7803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: -0.2015 S13: 0.3350
REMARK 3 S21: -0.2586 S22: 0.0465 S23: -0.2539
REMARK 3 S31: 0.3369 S32: 0.4665 S33: -0.0068
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND RESID 236 - 258
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8426 15.5668 40.7294
REMARK 3 T TENSOR
REMARK 3 T11: 0.2803 T22: 0.5669
REMARK 3 T33: -0.5385 T12: 0.2449
REMARK 3 T13: -0.0799 T23: 0.0559
REMARK 3 L TENSOR
REMARK 3 L11: 6.2662 L22: 0.1359
REMARK 3 L33: 12.7703 L12: -1.6304
REMARK 3 L13: -2.8760 L23: 2.8247
REMARK 3 S TENSOR
REMARK 3 S11: 0.0648 S12: -0.2799 S13: -0.0535
REMARK 3 S21: 0.1564 S22: 0.0065 S23: 0.0544
REMARK 3 S31: -0.1163 S32: -0.1027 S33: -0.0713
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND RESID 259 - 291
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0067 9.2723 35.1859
REMARK 3 T TENSOR
REMARK 3 T11: 0.4358 T22: 0.4041
REMARK 3 T33: -0.5366 T12: 0.3040
REMARK 3 T13: -0.1811 T23: 0.1307
REMARK 3 L TENSOR
REMARK 3 L11: 5.5534 L22: 4.7863
REMARK 3 L33: 10.1433 L12: -5.3824
REMARK 3 L13: -5.1474 L23: -0.7805
REMARK 3 S TENSOR
REMARK 3 S11: 0.1175 S12: -0.3720 S13: -0.3699
REMARK 3 S21: 0.0135 S22: -0.1559 S23: -0.4374
REMARK 3 S31: 0.0594 S32: 0.4873 S33: 0.0384
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND RESID 292 - 316
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1823 14.6538 25.8950
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.5582
REMARK 3 T33: -0.3229 T12: 0.2410
REMARK 3 T13: -0.0937 T23: 0.0771
REMARK 3 L TENSOR
REMARK 3 L11: 3.6129 L22: 1.5924
REMARK 3 L33: 8.9378 L12: -5.1963
REMARK 3 L13: -0.4360 L23: -3.2331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: -0.5617 S13: 0.0360
REMARK 3 S21: 0.1868 S22: -0.1780 S23: -0.1550
REMARK 3 S31: -0.2168 S32: 0.6054 S33: 0.1162
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND RESID 317 - 355
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5855 14.7447 14.7947
REMARK 3 T TENSOR
REMARK 3 T11: -0.1235 T22: 0.1169
REMARK 3 T33: -0.2874 T12: 0.1243
REMARK 3 T13: -0.0192 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 3.2070 L22: 8.7504
REMARK 3 L33: 13.3758 L12: -4.4780
REMARK 3 L13: 0.4018 L23: 0.1371
REMARK 3 S TENSOR
REMARK 3 S11: -0.1296 S12: -0.7003 S13: 0.0066
REMARK 3 S21: 0.7223 S22: 0.0231 S23: -0.1273
REMARK 3 S31: 0.2946 S32: 0.6252 S33: 0.1065
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND RESID 356 - 380
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7286 17.1256 9.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0187 T22: 0.1068
REMARK 3 T33: -0.0848 T12: 0.0318
REMARK 3 T13: 0.0810 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 6.3357 L22: 2.4681
REMARK 3 L33: 11.6809 L12: -4.5151
REMARK 3 L13: 0.9665 L23: -4.4932
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: -0.4406 S13: -0.0666
REMARK 3 S21: 0.1556 S22: 0.2994 S23: 0.1217
REMARK 3 S31: 0.2216 S32: -0.2456 S33: -0.2401
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND RESID 381 - 417
REMARK 3 ORIGIN FOR THE GROUP (A): -42.8892 19.8325 -2.4837
REMARK 3 T TENSOR
REMARK 3 T11: -0.0732 T22: -0.1780
REMARK 3 T33: 0.1305 T12: -0.0439
REMARK 3 T13: -0.0143 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 8.6556 L22: 4.3007
REMARK 3 L33: 8.8866 L12: -2.2263
REMARK 3 L13: -2.9866 L23: -1.9595
REMARK 3 S TENSOR
REMARK 3 S11: -0.1230 S12: 0.5162 S13: -0.4909
REMARK 3 S21: -0.2866 S22: -0.0896 S23: 0.7216
REMARK 3 S31: 0.2057 S32: -0.6902 S33: 0.2126
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND RESID 418 - 443
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3508 27.4487 -3.7739
REMARK 3 T TENSOR
REMARK 3 T11: 0.1557 T22: 0.4477
REMARK 3 T33: 0.5310 T12: 0.2150
REMARK 3 T13: -0.2247 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 7.9042 L22: 2.6206
REMARK 3 L33: 0.3800 L12: -3.6524
REMARK 3 L13: 2.0092 L23: 2.2479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: -0.1662 S13: -0.0382
REMARK 3 S21: -0.0533 S22: -0.1272 S23: 0.0632
REMARK 3 S31: 0.0704 S32: -0.1833 S33: 0.0992
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND RESID 444 - 468
REMARK 3 ORIGIN FOR THE GROUP (A): -41.6993 29.7475 2.8224
REMARK 3 T TENSOR
REMARK 3 T11: -0.1804 T22: -0.3723
REMARK 3 T33: 0.1492 T12: -0.0426
REMARK 3 T13: -0.0088 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 13.3477 L22: 9.4846
REMARK 3 L33: 6.9357 L12: -5.2883
REMARK 3 L13: 2.8301 L23: -1.8154
REMARK 3 S TENSOR
REMARK 3 S11: -0.0722 S12: -0.1821 S13: 0.7678
REMARK 3 S21: 0.5261 S22: -0.0020 S23: 0.0451
REMARK 3 S31: -0.3179 S32: -0.0114 S33: 0.0742
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND RESID 469 - 477
REMARK 3 ORIGIN FOR THE GROUP (A): -49.3496 31.0431 3.5278
REMARK 3 T TENSOR
REMARK 3 T11: -0.1860 T22: -0.2168
REMARK 3 T33: 0.3887 T12: 0.0358
REMARK 3 T13: -0.0969 T23: -0.2403
REMARK 3 L TENSOR
REMARK 3 L11: 2.6101 L22: 1.1613
REMARK 3 L33: 6.2608 L12: -1.8207
REMARK 3 L13: 1.3714 L23: 5.1597
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: 0.0896 S13: 0.1069
REMARK 3 S21: 0.1170 S22: 0.0113 S23: -0.0271
REMARK 3 S31: -0.2595 S32: 0.0807 S33: -0.0262
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN X AND RESID 203 - 213
REMARK 3 ORIGIN FOR THE GROUP (A): -32.7955 13.0120 64.2999
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.4383
REMARK 3 T33: -0.4399 T12: 0.0555
REMARK 3 T13: -0.0777 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.8656 L22: 5.9953
REMARK 3 L33: 8.3155 L12: 1.4886
REMARK 3 L13: -5.7296 L23: 1.6183
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: 0.0494 S13: -0.0471
REMARK 3 S21: -0.1059 S22: 0.1381 S23: 0.0234
REMARK 3 S31: 0.1765 S32: -0.0463 S33: -0.1298
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN Y AND RESID 203 - 212
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0868 14.6641 28.3493
REMARK 3 T TENSOR
REMARK 3 T11: 0.4413 T22: 0.4817
REMARK 3 T33: -0.3874 T12: 0.2550
REMARK 3 T13: 0.1330 T23: 0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 5.3015 L22: 0.0000
REMARK 3 L33: 5.0765 L12: 0.7055
REMARK 3 L13: 3.9038 L23: 3.7950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.0496 S13: -0.0389
REMARK 3 S21: -0.0629 S22: 0.0823 S23: 0.1102
REMARK 3 S31: -0.0092 S32: -0.0051 S33: -0.0748
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1290055103.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17034
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 54.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.04
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3CEQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10 M MES PH 6.5, 0.2 L-PROLINE, 7%
REMARK 280 PGA
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 43.90500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.90500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.43000
REMARK 290 SMTRY3 4 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: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y
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 VAL A 218
REMARK 465 PRO A 219
REMARK 465 LEU A 220
REMARK 465 CYS A 221
REMARK 465 LYS A 222
REMARK 465 GLN A 223
REMARK 465 ALA A 224
REMARK 465 LEU A 225
REMARK 465 GLU A 226
REMARK 465 ASP A 227
REMARK 465 LEU A 228
REMARK 465 GLU A 229
REMARK 465 LYS A 230
REMARK 465 THR A 231
REMARK 465 SER A 232
REMARK 465 GLY A 233
REMARK 465 HIS A 234
REMARK 465 ASP A 235
REMARK 465 LYS A 422
REMARK 465 ASP A 423
REMARK 465 LYS A 424
REMARK 465 ARG A 425
REMARK 465 ARG A 426
REMARK 465 ASP A 427
REMARK 465 SER A 428
REMARK 465 ALA A 429
REMARK 465 PRO A 430
REMARK 465 TYR A 431
REMARK 465 GLY A 432
REMARK 465 GLU A 433
REMARK 465 TYR A 434
REMARK 465 GLY A 435
REMARK 465 SER A 436
REMARK 465 TRP A 437
REMARK 465 TYR A 438
REMARK 465 LYS A 439
REMARK 465 LYS A 480
REMARK 465 VAL B 218
REMARK 465 PRO B 219
REMARK 465 LEU B 220
REMARK 465 CYS B 221
REMARK 465 LYS B 222
REMARK 465 GLN B 223
REMARK 465 ALA B 224
REMARK 465 LEU B 225
REMARK 465 GLU B 226
REMARK 465 ASP B 227
REMARK 465 LEU B 228
REMARK 465 GLU B 229
REMARK 465 LYS B 230
REMARK 465 THR B 231
REMARK 465 SER B 232
REMARK 465 GLY B 233
REMARK 465 HIS B 234
REMARK 465 ASP B 235
REMARK 465 LYS B 422
REMARK 465 ASP B 423
REMARK 465 LYS B 424
REMARK 465 ARG B 425
REMARK 465 ARG B 426
REMARK 465 ASP B 427
REMARK 465 SER B 428
REMARK 465 ALA B 429
REMARK 465 PRO B 430
REMARK 465 TYR B 431
REMARK 465 GLY B 432
REMARK 465 GLU B 433
REMARK 465 TYR B 434
REMARK 465 GLY B 435
REMARK 465 SER B 436
REMARK 465 TRP B 437
REMARK 465 TYR B 438
REMARK 465 SER B 478
REMARK 465 ARG B 479
REMARK 465 LYS B 480
REMARK 465 MET X 182
REMARK 465 GLY X 183
REMARK 465 SER X 184
REMARK 465 SER X 185
REMARK 465 HIS X 186
REMARK 465 HIS X 187
REMARK 465 HIS X 188
REMARK 465 HIS X 189
REMARK 465 HIS X 190
REMARK 465 HIS X 191
REMARK 465 SER X 192
REMARK 465 SER X 193
REMARK 465 GLY X 194
REMARK 465 LEU X 195
REMARK 465 VAL X 196
REMARK 465 PRO X 197
REMARK 465 ARG X 198
REMARK 465 GLY X 199
REMARK 465 SER X 200
REMARK 465 HIS X 201
REMARK 465 MET X 202
REMARK 465 GLY X 214
REMARK 465 SER X 215
REMARK 465 THR X 216
REMARK 465 GLY X 217
REMARK 465 SER X 218
REMARK 465 THR X 219
REMARK 465 GLY X 220
REMARK 465 SER X 221
REMARK 465 THR X 222
REMARK 465 GLY X 223
REMARK 465 SER X 224
REMARK 465 HIS X 225
REMARK 465 MET X 226
REMARK 465 MET Y 182
REMARK 465 GLY Y 183
REMARK 465 SER Y 184
REMARK 465 SER Y 185
REMARK 465 HIS Y 186
REMARK 465 HIS Y 187
REMARK 465 HIS Y 188
REMARK 465 HIS Y 189
REMARK 465 HIS Y 190
REMARK 465 HIS Y 191
REMARK 465 SER Y 192
REMARK 465 SER Y 193
REMARK 465 GLY Y 194
REMARK 465 LEU Y 195
REMARK 465 VAL Y 196
REMARK 465 PRO Y 197
REMARK 465 ARG Y 198
REMARK 465 GLY Y 199
REMARK 465 SER Y 200
REMARK 465 HIS Y 201
REMARK 465 MET Y 202
REMARK 465 THR Y 213
REMARK 465 GLY Y 214
REMARK 465 SER Y 215
REMARK 465 THR Y 216
REMARK 465 GLY Y 217
REMARK 465 SER Y 218
REMARK 465 THR Y 219
REMARK 465 GLY Y 220
REMARK 465 SER Y 221
REMARK 465 THR Y 222
REMARK 465 GLY Y 223
REMARK 465 SER Y 224
REMARK 465 HIS Y 225
REMARK 465 MET Y 226
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 ASP A 277 38.02 70.82
REMARK 500 ASN A 405 -138.20 -121.75
REMARK 500 GLU A 420 -6.26 -58.49
REMARK 500 CYS A 441 -76.91 -109.28
REMARK 500 LYS A 442 58.05 37.36
REMARK 500 ASP B 277 38.22 70.99
REMARK 500 ASN B 405 -137.24 -122.37
REMARK 500 GLU B 420 -7.66 -58.04
REMARK 500 CYS B 441 -91.49 -145.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES MGSSHHHHHHSSGLVPRGSHM AND TGSTGSTGSTGSHM ARE
REMARK 999 DERIVED FROM THE CLONING STRATEGY. ONLY RESIDUES
REMARK 999 TNLEWDDSAI BELONG TO Q8IWE5
DBREF 3ZFW A 218 480 UNP Q91YS4 Q91YS4_MOUSE 218 480
DBREF 3ZFW B 218 480 UNP Q91YS4 Q91YS4_MOUSE 218 480
DBREF 3ZFW X 203 212 UNP Q8IWE5 PKHM2_HUMAN 203 212
DBREF 3ZFW Y 203 212 UNP Q8IWE5 PKHM2_HUMAN 203 212
SEQADV 3ZFW MET X 182 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 183 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 184 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 185 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 186 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 187 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 188 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 189 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 190 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 191 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 192 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 193 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 194 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW LEU X 195 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW VAL X 196 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW PRO X 197 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW ARG X 198 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 199 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 200 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 201 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW MET X 202 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR X 213 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 214 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 215 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR X 216 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 217 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 218 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR X 219 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 220 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 221 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR X 222 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY X 223 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER X 224 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS X 225 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW MET X 226 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW MET Y 182 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 183 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 184 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 185 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 186 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 187 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 188 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 189 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 190 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 191 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 192 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 193 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 194 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW LEU Y 195 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW VAL Y 196 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW PRO Y 197 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW ARG Y 198 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 199 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 200 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 201 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW MET Y 202 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR Y 213 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 214 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 215 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR Y 216 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 217 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 218 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR Y 219 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 220 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 221 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW THR Y 222 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW GLY Y 223 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW SER Y 224 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW HIS Y 225 UNP Q81WE5 EXPRESSION TAG
SEQADV 3ZFW MET Y 226 UNP Q81WE5 EXPRESSION TAG
SEQRES 1 A 263 VAL PRO LEU CYS LYS GLN ALA LEU GLU ASP LEU GLU LYS
SEQRES 2 A 263 THR SER GLY HIS ASP HIS PRO ASP VAL ALA THR MET LEU
SEQRES 3 A 263 ASN ILE LEU ALA LEU VAL TYR ARG ASP GLN ASN LYS TYR
SEQRES 4 A 263 LYS ASP ALA ALA HIS LEU LEU ASN ASP ALA LEU ALA ILE
SEQRES 5 A 263 ARG GLU LYS THR LEU GLY LYS ASP HIS PRO ALA VAL ALA
SEQRES 6 A 263 ALA THR LEU ASN ASN LEU ALA VAL LEU TYR GLY LYS ARG
SEQRES 7 A 263 GLY LYS TYR LYS GLU ALA GLU PRO LEU CYS LYS ARG ALA
SEQRES 8 A 263 LEU GLU ILE ARG GLU LYS VAL LEU GLY LYS PHE HIS PRO
SEQRES 9 A 263 ASP VAL ALA LYS GLN LEU SER ASN LEU ALA LEU LEU CYS
SEQRES 10 A 263 GLN ASN GLN GLY LYS ALA GLU GLU VAL GLU TYR TYR TYR
SEQRES 11 A 263 ARG ARG ALA LEU GLU ILE TYR ALA THR ARG LEU GLY PRO
SEQRES 12 A 263 ASP ASP PRO ASN VAL ALA LYS THR LYS ASN ASN LEU ALA
SEQRES 13 A 263 SER CYS TYR LEU LYS GLN GLY LYS TYR GLN ASP ALA GLU
SEQRES 14 A 263 THR LEU TYR LYS GLU ILE LEU THR ARG ALA HIS GLU LYS
SEQRES 15 A 263 GLU PHE GLY SER VAL ASN GLY GLU ASN LYS PRO ILE TRP
SEQRES 16 A 263 MET HIS ALA GLU GLU ARG GLU GLU SER LYS ASP LYS ARG
SEQRES 17 A 263 ARG ASP SER ALA PRO TYR GLY GLU TYR GLY SER TRP TYR
SEQRES 18 A 263 LYS ALA CYS LYS VAL ASP SER PRO THR VAL ASN THR THR
SEQRES 19 A 263 LEU ARG SER LEU GLY ALA LEU TYR ARG ARG GLN GLY LYS
SEQRES 20 A 263 LEU GLU ALA ALA HIS THR LEU GLU ASP CYS ALA SER ARG
SEQRES 21 A 263 SER ARG LYS
SEQRES 1 B 263 VAL PRO LEU CYS LYS GLN ALA LEU GLU ASP LEU GLU LYS
SEQRES 2 B 263 THR SER GLY HIS ASP HIS PRO ASP VAL ALA THR MET LEU
SEQRES 3 B 263 ASN ILE LEU ALA LEU VAL TYR ARG ASP GLN ASN LYS TYR
SEQRES 4 B 263 LYS ASP ALA ALA HIS LEU LEU ASN ASP ALA LEU ALA ILE
SEQRES 5 B 263 ARG GLU LYS THR LEU GLY LYS ASP HIS PRO ALA VAL ALA
SEQRES 6 B 263 ALA THR LEU ASN ASN LEU ALA VAL LEU TYR GLY LYS ARG
SEQRES 7 B 263 GLY LYS TYR LYS GLU ALA GLU PRO LEU CYS LYS ARG ALA
SEQRES 8 B 263 LEU GLU ILE ARG GLU LYS VAL LEU GLY LYS PHE HIS PRO
SEQRES 9 B 263 ASP VAL ALA LYS GLN LEU SER ASN LEU ALA LEU LEU CYS
SEQRES 10 B 263 GLN ASN GLN GLY LYS ALA GLU GLU VAL GLU TYR TYR TYR
SEQRES 11 B 263 ARG ARG ALA LEU GLU ILE TYR ALA THR ARG LEU GLY PRO
SEQRES 12 B 263 ASP ASP PRO ASN VAL ALA LYS THR LYS ASN ASN LEU ALA
SEQRES 13 B 263 SER CYS TYR LEU LYS GLN GLY LYS TYR GLN ASP ALA GLU
SEQRES 14 B 263 THR LEU TYR LYS GLU ILE LEU THR ARG ALA HIS GLU LYS
SEQRES 15 B 263 GLU PHE GLY SER VAL ASN GLY GLU ASN LYS PRO ILE TRP
SEQRES 16 B 263 MET HIS ALA GLU GLU ARG GLU GLU SER LYS ASP LYS ARG
SEQRES 17 B 263 ARG ASP SER ALA PRO TYR GLY GLU TYR GLY SER TRP TYR
SEQRES 18 B 263 LYS ALA CYS LYS VAL ASP SER PRO THR VAL ASN THR THR
SEQRES 19 B 263 LEU ARG SER LEU GLY ALA LEU TYR ARG ARG GLN GLY LYS
SEQRES 20 B 263 LEU GLU ALA ALA HIS THR LEU GLU ASP CYS ALA SER ARG
SEQRES 21 B 263 SER ARG LYS
SEQRES 1 X 45 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 X 45 LEU VAL PRO ARG GLY SER HIS MET THR ASN LEU GLU TRP
SEQRES 3 X 45 ASP ASP SER ALA ILE THR GLY SER THR GLY SER THR GLY
SEQRES 4 X 45 SER THR GLY SER HIS MET
SEQRES 1 Y 45 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 Y 45 LEU VAL PRO ARG GLY SER HIS MET THR ASN LEU GLU TRP
SEQRES 3 Y 45 ASP ASP SER ALA ILE THR GLY SER THR GLY SER THR GLY
SEQRES 4 Y 45 SER THR GLY SER HIS MET
HELIX 1 1 HIS A 236 GLN A 253 1 18
HELIX 2 2 LYS A 255 LEU A 274 1 20
HELIX 3 3 HIS A 278 ARG A 295 1 18
HELIX 4 4 LYS A 297 LEU A 316 1 20
HELIX 5 5 HIS A 320 ASN A 336 1 17
HELIX 6 6 LYS A 339 LEU A 358 1 20
HELIX 7 7 ASP A 362 GLN A 379 1 18
HELIX 8 8 LYS A 381 GLY A 402 1 22
HELIX 9 9 PRO A 410 GLU A 420 1 11
HELIX 10 10 SER A 445 GLN A 462 1 18
HELIX 11 11 LYS A 464 ARG A 479 1 16
HELIX 12 12 HIS B 236 GLN B 253 1 18
HELIX 13 13 LYS B 255 LEU B 274 1 20
HELIX 14 14 HIS B 278 ARG B 295 1 18
HELIX 15 15 LYS B 297 LEU B 316 1 20
HELIX 16 16 HIS B 320 ASN B 336 1 17
HELIX 17 17 LYS B 339 LEU B 358 1 20
HELIX 18 18 ASP B 362 GLN B 379 1 18
HELIX 19 19 LYS B 381 GLY B 402 1 22
HELIX 20 20 PRO B 410 GLU B 420 1 11
HELIX 21 21 SER B 445 GLN B 462 1 18
HELIX 22 22 LYS B 464 SER B 476 1 13
SSBOND 1 CYS A 441 CYS A 474 1555 1555 2.05
SSBOND 2 CYS B 441 CYS B 474 1555 1555 2.04
CRYST1 87.810 90.860 94.040 90.00 90.00 90.00 P 21 21 2 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 0.011388 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010634 0.00000
MTRIX1 1 0.177700 0.984100 -0.000756 -40.50000 1
MTRIX2 1 0.984100 -0.177700 0.000105 48.13000 1
MTRIX3 1 0.000000 0.000000 -1.000000 93.09000 1
MTRIX1 2 0.199700 0.979800 -0.014070 -39.26000 1
MTRIX2 2 0.979800 -0.199400 0.016500 48.07000 1
MTRIX3 2 0.013360 -0.017080 -0.999800 93.69000 1
(ATOM LINES ARE NOT SHOWN.)
END
