HEADER OXIDOREDUCTASE 24-MAR-11 3R8W
TITLE STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE ISOFORM 2 FROM
TITLE 2 ARABIDOPSIS THALIANA AT 2.2 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE 2, CHLOROPLASTIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 3-IPM-DH 2, IMDH 2, BETA-IPM DEHYDROGENASE 2;
COMPND 5 EC: 1.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT1G80560, IMDH, IMDH2, T21F11.11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS8
KEYWDS DIMER, ISOCITRATE AND ISOPROPYLMALATE DEHYDROGENASES FAMILY, LEUCINE
KEYWDS 2 BIOSYNTHESIS, GLUCOSINOLATE BIOSYNTHESIS, NADH, 3-ISOPROPYLMALATE,
KEYWDS 3 CHLOROPLAST, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.HE,A.GALANT,Q.PANG,J.M.STRUL,S.BALOGUN,J.M.JEZ,S.CHEN
REVDAT 3 21-FEB-24 3R8W 1 REMARK
REVDAT 2 04-APR-12 3R8W 1 JRNL VERSN
REVDAT 1 22-JUN-11 3R8W 0
JRNL AUTH Y.HE,A.GALANT,Q.PANG,J.M.STRUL,S.F.BALOGUN,J.M.JEZ,S.CHEN
JRNL TITL STRUCTURAL AND FUNCTIONAL EVOLUTION OF ISOPROPYLMALATE
JRNL TITL 2 DEHYDROGENASES IN THE LEUCINE AND GLUCOSINOLATE PATHWAYS OF
JRNL TITL 3 ARABIDOPSIS THALIANA.
JRNL REF J.BIOL.CHEM. V. 286 28794 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21697089
JRNL DOI 10.1074/JBC.M111.262519
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.2_432)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 107153
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 5388
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.0030 - 4.8443 0.97 10712 582 0.1625 0.1891
REMARK 3 2 4.8443 - 3.8463 0.99 10911 582 0.1340 0.1572
REMARK 3 3 3.8463 - 3.3605 0.99 10869 578 0.1821 0.2108
REMARK 3 4 3.3605 - 3.0534 0.98 10774 545 0.1862 0.2247
REMARK 3 5 3.0534 - 2.8346 0.96 10536 555 0.1996 0.2354
REMARK 3 6 2.8346 - 2.6676 0.94 10271 562 0.2092 0.2527
REMARK 3 7 2.6676 - 2.5340 0.92 10079 517 0.2136 0.2641
REMARK 3 8 2.5340 - 2.4237 0.89 9680 512 0.2195 0.2829
REMARK 3 9 2.4237 - 2.3304 0.83 9037 517 0.2568 0.3200
REMARK 3 10 2.3304 - 2.2500 0.81 8896 438 0.2634 0.2997
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 59.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.69100
REMARK 3 B22 (A**2) : -6.63720
REMARK 3 B33 (A**2) : 3.94620
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15010
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 11146
REMARK 3 ANGLE : 0.980 15072
REMARK 3 CHIRALITY : 0.061 1729
REMARK 3 PLANARITY : 0.004 2000
REMARK 3 DIHEDRAL : 12.366 4170
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 3:106
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7303 -24.5497 10.4072
REMARK 3 T TENSOR
REMARK 3 T11: 0.4007 T22: 0.2748
REMARK 3 T33: 0.4533 T12: -0.0406
REMARK 3 T13: 0.0045 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 3.8466 L22: 1.6655
REMARK 3 L33: 2.2208 L12: 2.2509
REMARK 3 L13: -1.0517 L23: -0.7410
REMARK 3 S TENSOR
REMARK 3 S11: -0.2168 S12: 0.1488 S13: -0.3593
REMARK 3 S21: -0.1626 S22: 0.2793 S23: 0.0034
REMARK 3 S31: 0.2828 S32: -0.2377 S33: -0.0331
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 107:261
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0714 -8.5805 23.7445
REMARK 3 T TENSOR
REMARK 3 T11: 0.3556 T22: 0.4304
REMARK 3 T33: 0.4177 T12: 0.0365
REMARK 3 T13: 0.0371 T23: 0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 0.7549 L22: 2.0151
REMARK 3 L33: 1.1164 L12: -0.0521
REMARK 3 L13: 0.0678 L23: -0.2233
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.1074 S13: -0.1839
REMARK 3 S21: 0.1516 S22: 0.1905 S23: -0.0704
REMARK 3 S31: 0.0623 S32: -0.0737 S33: -0.1559
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 262:360
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7118 -22.4222 3.3960
REMARK 3 T TENSOR
REMARK 3 T11: 0.4504 T22: 0.3931
REMARK 3 T33: 0.5187 T12: -0.0207
REMARK 3 T13: 0.1051 T23: -0.1076
REMARK 3 L TENSOR
REMARK 3 L11: 2.0123 L22: 2.0443
REMARK 3 L33: 2.2709 L12: 1.4514
REMARK 3 L13: -1.1393 L23: 0.8158
REMARK 3 S TENSOR
REMARK 3 S11: -0.2610 S12: 0.1848 S13: -0.6137
REMARK 3 S21: -0.3317 S22: 0.3498 S23: -0.3490
REMARK 3 S31: 0.1346 S32: 0.0357 S33: -0.0144
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 3:103
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3174 24.3592 32.9277
REMARK 3 T TENSOR
REMARK 3 T11: 0.5034 T22: 0.3165
REMARK 3 T33: 0.4538 T12: 0.0224
REMARK 3 T13: 0.0192 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 2.2420 L22: 1.1178
REMARK 3 L33: 4.2315 L12: -0.4821
REMARK 3 L13: -0.7455 L23: 2.0394
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: -0.2075 S13: 0.2462
REMARK 3 S21: 0.0307 S22: 0.3200 S23: -0.1403
REMARK 3 S31: -0.3513 S32: 0.2340 S33: -0.2010
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESID 104:261
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6029 8.3534 17.4402
REMARK 3 T TENSOR
REMARK 3 T11: 0.4205 T22: 0.4162
REMARK 3 T33: 0.3416 T12: 0.0605
REMARK 3 T13: 0.0315 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 1.1332 L22: 1.9737
REMARK 3 L33: 1.0806 L12: -0.0855
REMARK 3 L13: -0.0581 L23: -0.1095
REMARK 3 S TENSOR
REMARK 3 S11: -0.1969 S12: -0.0957 S13: 0.0719
REMARK 3 S21: -0.0458 S22: 0.2270 S23: 0.1490
REMARK 3 S31: -0.2048 S32: -0.0620 S33: -0.0261
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESID 262:360
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2189 21.9986 17.5082
REMARK 3 T TENSOR
REMARK 3 T11: 0.5859 T22: 0.4215
REMARK 3 T33: 0.5113 T12: -0.1057
REMARK 3 T13: 0.1132 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.4135 L22: 1.9245
REMARK 3 L33: 2.3895 L12: 0.3920
REMARK 3 L13: -1.0142 L23: 1.3412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: -0.0109 S13: 0.1363
REMARK 3 S21: -0.3785 S22: 0.3707 S23: -0.4166
REMARK 3 S31: -0.6504 S32: 0.2208 S33: -0.3385
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND RESID 3:103
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9965 -77.5192 5.5357
REMARK 3 T TENSOR
REMARK 3 T11: 0.4841 T22: 0.2782
REMARK 3 T33: 0.4399 T12: -0.0197
REMARK 3 T13: -0.0241 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 2.1880 L22: 1.1412
REMARK 3 L33: 4.4384 L12: 0.4448
REMARK 3 L13: 1.1254 L23: 2.1099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.2256 S13: -0.3265
REMARK 3 S21: -0.0058 S22: 0.2513 S23: -0.2091
REMARK 3 S31: 0.4744 S32: 0.1598 S33: -0.2218
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND RESID 104:261
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7753 -61.4992 20.9912
REMARK 3 T TENSOR
REMARK 3 T11: 0.3962 T22: 0.4061
REMARK 3 T33: 0.3261 T12: -0.0608
REMARK 3 T13: -0.0319 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 1.3426 L22: 2.2263
REMARK 3 L33: 0.8035 L12: -0.0421
REMARK 3 L13: 0.1583 L23: -0.1815
REMARK 3 S TENSOR
REMARK 3 S11: -0.1747 S12: 0.1019 S13: -0.0683
REMARK 3 S21: 0.0254 S22: 0.2080 S23: 0.1403
REMARK 3 S31: 0.1941 S32: -0.0504 S33: -0.0396
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND RESID 262:360
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2721 -75.2580 20.9349
REMARK 3 T TENSOR
REMARK 3 T11: 0.5621 T22: 0.4364
REMARK 3 T33: 0.4676 T12: 0.1004
REMARK 3 T13: -0.0874 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.2603 L22: 2.0762
REMARK 3 L33: 2.0985 L12: -0.9124
REMARK 3 L13: 1.0065 L23: 1.2283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0917 S12: 0.0078 S13: -0.2074
REMARK 3 S21: 0.3000 S22: 0.3387 S23: -0.3613
REMARK 3 S31: 0.6109 S32: 0.2134 S33: -0.2878
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN D AND RESID 3:103
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9385 -28.3986 28.4276
REMARK 3 T TENSOR
REMARK 3 T11: 0.4257 T22: 0.2841
REMARK 3 T33: 0.4788 T12: 0.0441
REMARK 3 T13: -0.0338 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 4.1637 L22: 1.0085
REMARK 3 L33: 2.4962 L12: -1.8888
REMARK 3 L13: 0.7685 L23: -0.7003
REMARK 3 S TENSOR
REMARK 3 S11: -0.2858 S12: -0.1927 S13: 0.3463
REMARK 3 S21: 0.1224 S22: 0.3131 S23: 0.1071
REMARK 3 S31: -0.2788 S32: -0.2227 S33: -0.0228
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN D AND RESID 104:261
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4814 -44.4308 14.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.3516 T22: 0.4286
REMARK 3 T33: 0.4103 T12: -0.0375
REMARK 3 T13: -0.0357 T23: 0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 0.9978 L22: 2.1636
REMARK 3 L33: 1.3263 L12: 0.2370
REMARK 3 L13: 0.1646 L23: 0.0642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.0477 S13: 0.1934
REMARK 3 S21: -0.1072 S22: 0.2504 S23: -0.0302
REMARK 3 S31: -0.0947 S32: -0.0908 S33: -0.1728
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN D AND RESID 262:360
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5721 -30.6714 35.2095
REMARK 3 T TENSOR
REMARK 3 T11: 0.4676 T22: 0.3961
REMARK 3 T33: 0.5467 T12: 0.0288
REMARK 3 T13: -0.0963 T23: -0.1117
REMARK 3 L TENSOR
REMARK 3 L11: 2.3566 L22: 2.0152
REMARK 3 L33: 2.2538 L12: -1.2646
REMARK 3 L13: 1.5328 L23: 0.7649
REMARK 3 S TENSOR
REMARK 3 S11: -0.3130 S12: -0.2103 S13: 0.6989
REMARK 3 S21: 0.4096 S22: 0.3336 S23: -0.3183
REMARK 3 S31: -0.1458 S32: 0.0451 S33: 0.0584
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064636.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.68
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR.
REMARK 200 LN2 COOLED FIRST CRYSTAL,
REMARK 200 SAGITTAL FOCUSING 2ND CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114991
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 20% GLYCEROL, 0.16M
REMARK 280 AMMONIUM SULFATE, 0.08 SODIUM ACETATE TRIHYDRATE , PH 4.68,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 105.50800
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: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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: 5260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 MET A -37
REMARK 465 ALA A -36
REMARK 465 ALA A -35
REMARK 465 ALA A -34
REMARK 465 LEU A -33
REMARK 465 GLN A -32
REMARK 465 THR A -31
REMARK 465 ASN A -30
REMARK 465 ILE A -29
REMARK 465 ARG A -28
REMARK 465 THR A -27
REMARK 465 VAL A -26
REMARK 465 LYS A -25
REMARK 465 VAL A -24
REMARK 465 PRO A -23
REMARK 465 ALA A -22
REMARK 465 THR A -21
REMARK 465 PHE A -20
REMARK 465 ARG A -19
REMARK 465 ALA A -18
REMARK 465 VAL A -17
REMARK 465 SER A -16
REMARK 465 LYS A -15
REMARK 465 GLN A -14
REMARK 465 SER A -13
REMARK 465 LEU A -12
REMARK 465 ALA A -11
REMARK 465 PRO A -10
REMARK 465 PHE A -9
REMARK 465 ARG A -8
REMARK 465 VAL A -7
REMARK 465 ARG A -6
REMARK 465 CYS A -5
REMARK 465 ALA A -4
REMARK 465 VAL A -3
REMARK 465 ALA A -2
REMARK 465 SER A -1
REMARK 465 PRO A 0
REMARK 465 GLY A 1
REMARK 465 LYS A 2
REMARK 465 SER A 361
REMARK 465 GLN A 362
REMARK 465 VAL A 363
REMARK 465 PRO A 364
REMARK 465 ALA A 365
REMARK 465 SER A 366
REMARK 465 VAL A 367
REMARK 465 MET B -37
REMARK 465 ALA B -36
REMARK 465 ALA B -35
REMARK 465 ALA B -34
REMARK 465 LEU B -33
REMARK 465 GLN B -32
REMARK 465 THR B -31
REMARK 465 ASN B -30
REMARK 465 ILE B -29
REMARK 465 ARG B -28
REMARK 465 THR B -27
REMARK 465 VAL B -26
REMARK 465 LYS B -25
REMARK 465 VAL B -24
REMARK 465 PRO B -23
REMARK 465 ALA B -22
REMARK 465 THR B -21
REMARK 465 PHE B -20
REMARK 465 ARG B -19
REMARK 465 ALA B -18
REMARK 465 VAL B -17
REMARK 465 SER B -16
REMARK 465 LYS B -15
REMARK 465 GLN B -14
REMARK 465 SER B -13
REMARK 465 LEU B -12
REMARK 465 ALA B -11
REMARK 465 PRO B -10
REMARK 465 PHE B -9
REMARK 465 ARG B -8
REMARK 465 VAL B -7
REMARK 465 ARG B -6
REMARK 465 CYS B -5
REMARK 465 ALA B -4
REMARK 465 VAL B -3
REMARK 465 ALA B -2
REMARK 465 SER B -1
REMARK 465 PRO B 0
REMARK 465 GLY B 1
REMARK 465 LYS B 2
REMARK 465 SER B 361
REMARK 465 GLN B 362
REMARK 465 VAL B 363
REMARK 465 PRO B 364
REMARK 465 ALA B 365
REMARK 465 SER B 366
REMARK 465 VAL B 367
REMARK 465 MET C -37
REMARK 465 ALA C -36
REMARK 465 ALA C -35
REMARK 465 ALA C -34
REMARK 465 LEU C -33
REMARK 465 GLN C -32
REMARK 465 THR C -31
REMARK 465 ASN C -30
REMARK 465 ILE C -29
REMARK 465 ARG C -28
REMARK 465 THR C -27
REMARK 465 VAL C -26
REMARK 465 LYS C -25
REMARK 465 VAL C -24
REMARK 465 PRO C -23
REMARK 465 ALA C -22
REMARK 465 THR C -21
REMARK 465 PHE C -20
REMARK 465 ARG C -19
REMARK 465 ALA C -18
REMARK 465 VAL C -17
REMARK 465 SER C -16
REMARK 465 LYS C -15
REMARK 465 GLN C -14
REMARK 465 SER C -13
REMARK 465 LEU C -12
REMARK 465 ALA C -11
REMARK 465 PRO C -10
REMARK 465 PHE C -9
REMARK 465 ARG C -8
REMARK 465 VAL C -7
REMARK 465 ARG C -6
REMARK 465 CYS C -5
REMARK 465 ALA C -4
REMARK 465 VAL C -3
REMARK 465 ALA C -2
REMARK 465 SER C -1
REMARK 465 PRO C 0
REMARK 465 GLY C 1
REMARK 465 LYS C 2
REMARK 465 SER C 361
REMARK 465 GLN C 362
REMARK 465 VAL C 363
REMARK 465 PRO C 364
REMARK 465 ALA C 365
REMARK 465 SER C 366
REMARK 465 VAL C 367
REMARK 465 MET D -37
REMARK 465 ALA D -36
REMARK 465 ALA D -35
REMARK 465 ALA D -34
REMARK 465 LEU D -33
REMARK 465 GLN D -32
REMARK 465 THR D -31
REMARK 465 ASN D -30
REMARK 465 ILE D -29
REMARK 465 ARG D -28
REMARK 465 THR D -27
REMARK 465 VAL D -26
REMARK 465 LYS D -25
REMARK 465 VAL D -24
REMARK 465 PRO D -23
REMARK 465 ALA D -22
REMARK 465 THR D -21
REMARK 465 PHE D -20
REMARK 465 ARG D -19
REMARK 465 ALA D -18
REMARK 465 VAL D -17
REMARK 465 SER D -16
REMARK 465 LYS D -15
REMARK 465 GLN D -14
REMARK 465 SER D -13
REMARK 465 LEU D -12
REMARK 465 ALA D -11
REMARK 465 PRO D -10
REMARK 465 PHE D -9
REMARK 465 ARG D -8
REMARK 465 VAL D -7
REMARK 465 ARG D -6
REMARK 465 CYS D -5
REMARK 465 ALA D -4
REMARK 465 VAL D -3
REMARK 465 ALA D -2
REMARK 465 SER D -1
REMARK 465 PRO D 0
REMARK 465 GLY D 1
REMARK 465 LYS D 2
REMARK 465 GLU D 154
REMARK 465 ASN D 155
REMARK 465 SER D 361
REMARK 465 GLN D 362
REMARK 465 VAL D 363
REMARK 465 PRO D 364
REMARK 465 ALA D 365
REMARK 465 SER D 366
REMARK 465 VAL D 367
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 O HOH C 461 O HOH C 463 1.91
REMARK 500 O HOH A 386 O HOH A 473 1.92
REMARK 500 NH1 ARG C 41 O HOH C 418 1.93
REMARK 500 O HOH A 448 O HOH A 449 1.94
REMARK 500 O HOH C 393 O HOH C 481 1.98
REMARK 500 O HOH A 467 O HOH A 469 1.99
REMARK 500 OE1 GLU D 18 O HOH D 470 1.99
REMARK 500 NH2 ARG D 41 O HOH D 425 2.05
REMARK 500 O HOH D 462 O HOH D 471 2.11
REMARK 500 O LYS C 309 O HOH C 446 2.14
REMARK 500 O VAL A 165 O HOH A 425 2.15
REMARK 500 O VAL C 165 O HOH C 434 2.17
REMARK 500 NH1 ARG B 334 OG SER B 340 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA D 341 CB - CA - C ANGL. DEV. = -19.4 DEGREES
REMARK 500 ALA D 341 N - CA - C ANGL. DEV. = 24.9 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 ASP A 131 87.76 -162.24
REMARK 500 ASN A 153 31.98 -84.92
REMARK 500 GLU A 154 -6.82 64.05
REMARK 500 ARG A 185 -103.18 -131.99
REMARK 500 VAL A 197 -44.29 -139.53
REMARK 500 ASP A 235 63.87 -155.05
REMARK 500 ASP A 240 -81.98 -105.52
REMARK 500 GLU A 314 72.27 -104.13
REMARK 500 LYS A 316 -68.19 74.53
REMARK 500 ASP B 131 88.08 -163.98
REMARK 500 ARG B 185 -105.92 -128.52
REMARK 500 VAL B 197 -42.51 -134.96
REMARK 500 ASP B 235 66.37 -158.57
REMARK 500 ASP B 240 -79.68 -107.24
REMARK 500 ALA B 286 62.00 39.13
REMARK 500 ASP C 131 88.68 -162.82
REMARK 500 ASN C 155 -19.36 89.67
REMARK 500 ARG C 185 -102.61 -131.19
REMARK 500 VAL C 197 -43.36 -136.73
REMARK 500 ASP C 235 65.55 -156.89
REMARK 500 ASP C 240 -82.83 -102.51
REMARK 500 GLU C 314 68.69 -104.92
REMARK 500 LYS C 316 -61.67 76.57
REMARK 500 ASP D 131 91.74 -161.35
REMARK 500 ARG D 185 -106.95 -129.61
REMARK 500 VAL D 197 -41.03 -137.46
REMARK 500 ASP D 235 66.09 -157.93
REMARK 500 ASP D 240 -81.87 -104.17
REMARK 500 GLU D 314 69.57 -107.04
REMARK 500 GLU D 315 177.73 -59.09
REMARK 500 LYS D 316 -70.36 76.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 370
DBREF 3R8W A -37 367 UNP P93832 LEU32_ARATH 1 405
DBREF 3R8W B -37 367 UNP P93832 LEU32_ARATH 1 405
DBREF 3R8W C -37 367 UNP P93832 LEU32_ARATH 1 405
DBREF 3R8W D -37 367 UNP P93832 LEU32_ARATH 1 405
SEQRES 1 A 405 MET ALA ALA ALA LEU GLN THR ASN ILE ARG THR VAL LYS
SEQRES 2 A 405 VAL PRO ALA THR PHE ARG ALA VAL SER LYS GLN SER LEU
SEQRES 3 A 405 ALA PRO PHE ARG VAL ARG CYS ALA VAL ALA SER PRO GLY
SEQRES 4 A 405 LYS LYS ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY
SEQRES 5 A 405 ILE GLY PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU
SEQRES 6 A 405 GLN GLN ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE
SEQRES 7 A 405 ARG GLU MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL
SEQRES 8 A 405 GLY VAL PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS
SEQRES 9 A 405 GLU SER ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR
SEQRES 10 A 405 LYS TRP ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS
SEQRES 11 A 405 GLY LEU LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA
SEQRES 12 A 405 ASN LEU ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP
SEQRES 13 A 405 ALA SER THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP
SEQRES 14 A 405 LEU MET VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE
SEQRES 15 A 405 GLY GLU PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU
SEQRES 16 A 405 GLU VAL GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU
SEQRES 17 A 405 ILE ASP ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG
SEQRES 18 A 405 LYS ARG ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN
SEQRES 19 A 405 VAL LEU GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR
SEQRES 20 A 405 ALA LEU ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS
SEQRES 21 A 405 MET TYR VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP
SEQRES 22 A 405 PRO LYS GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE
SEQRES 23 A 405 GLY ASP ILE LEU SER ASP GLU ALA SER MET ILE THR GLY
SEQRES 24 A 405 SER ILE GLY MET LEU PRO SER ALA SER LEU SER ASP SER
SEQRES 25 A 405 GLY PRO GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO
SEQRES 26 A 405 ASP ILE ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR
SEQRES 27 A 405 ILE LEU SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY
SEQRES 28 A 405 GLU GLU LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU
SEQRES 29 A 405 VAL ALA LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR
SEQRES 30 A 405 SER ALA GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY
SEQRES 31 A 405 GLU GLU VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA
SEQRES 32 A 405 SER VAL
SEQRES 1 B 405 MET ALA ALA ALA LEU GLN THR ASN ILE ARG THR VAL LYS
SEQRES 2 B 405 VAL PRO ALA THR PHE ARG ALA VAL SER LYS GLN SER LEU
SEQRES 3 B 405 ALA PRO PHE ARG VAL ARG CYS ALA VAL ALA SER PRO GLY
SEQRES 4 B 405 LYS LYS ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY
SEQRES 5 B 405 ILE GLY PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU
SEQRES 6 B 405 GLN GLN ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE
SEQRES 7 B 405 ARG GLU MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL
SEQRES 8 B 405 GLY VAL PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS
SEQRES 9 B 405 GLU SER ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR
SEQRES 10 B 405 LYS TRP ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS
SEQRES 11 B 405 GLY LEU LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA
SEQRES 12 B 405 ASN LEU ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP
SEQRES 13 B 405 ALA SER THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP
SEQRES 14 B 405 LEU MET VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE
SEQRES 15 B 405 GLY GLU PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU
SEQRES 16 B 405 GLU VAL GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU
SEQRES 17 B 405 ILE ASP ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG
SEQRES 18 B 405 LYS ARG ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN
SEQRES 19 B 405 VAL LEU GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR
SEQRES 20 B 405 ALA LEU ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS
SEQRES 21 B 405 MET TYR VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP
SEQRES 22 B 405 PRO LYS GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE
SEQRES 23 B 405 GLY ASP ILE LEU SER ASP GLU ALA SER MET ILE THR GLY
SEQRES 24 B 405 SER ILE GLY MET LEU PRO SER ALA SER LEU SER ASP SER
SEQRES 25 B 405 GLY PRO GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO
SEQRES 26 B 405 ASP ILE ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR
SEQRES 27 B 405 ILE LEU SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY
SEQRES 28 B 405 GLU GLU LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU
SEQRES 29 B 405 VAL ALA LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR
SEQRES 30 B 405 SER ALA GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY
SEQRES 31 B 405 GLU GLU VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA
SEQRES 32 B 405 SER VAL
SEQRES 1 C 405 MET ALA ALA ALA LEU GLN THR ASN ILE ARG THR VAL LYS
SEQRES 2 C 405 VAL PRO ALA THR PHE ARG ALA VAL SER LYS GLN SER LEU
SEQRES 3 C 405 ALA PRO PHE ARG VAL ARG CYS ALA VAL ALA SER PRO GLY
SEQRES 4 C 405 LYS LYS ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY
SEQRES 5 C 405 ILE GLY PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU
SEQRES 6 C 405 GLN GLN ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE
SEQRES 7 C 405 ARG GLU MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL
SEQRES 8 C 405 GLY VAL PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS
SEQRES 9 C 405 GLU SER ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR
SEQRES 10 C 405 LYS TRP ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS
SEQRES 11 C 405 GLY LEU LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA
SEQRES 12 C 405 ASN LEU ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP
SEQRES 13 C 405 ALA SER THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP
SEQRES 14 C 405 LEU MET VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE
SEQRES 15 C 405 GLY GLU PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU
SEQRES 16 C 405 GLU VAL GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU
SEQRES 17 C 405 ILE ASP ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG
SEQRES 18 C 405 LYS ARG ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN
SEQRES 19 C 405 VAL LEU GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR
SEQRES 20 C 405 ALA LEU ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS
SEQRES 21 C 405 MET TYR VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP
SEQRES 22 C 405 PRO LYS GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE
SEQRES 23 C 405 GLY ASP ILE LEU SER ASP GLU ALA SER MET ILE THR GLY
SEQRES 24 C 405 SER ILE GLY MET LEU PRO SER ALA SER LEU SER ASP SER
SEQRES 25 C 405 GLY PRO GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO
SEQRES 26 C 405 ASP ILE ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR
SEQRES 27 C 405 ILE LEU SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY
SEQRES 28 C 405 GLU GLU LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU
SEQRES 29 C 405 VAL ALA LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR
SEQRES 30 C 405 SER ALA GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY
SEQRES 31 C 405 GLU GLU VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA
SEQRES 32 C 405 SER VAL
SEQRES 1 D 405 MET ALA ALA ALA LEU GLN THR ASN ILE ARG THR VAL LYS
SEQRES 2 D 405 VAL PRO ALA THR PHE ARG ALA VAL SER LYS GLN SER LEU
SEQRES 3 D 405 ALA PRO PHE ARG VAL ARG CYS ALA VAL ALA SER PRO GLY
SEQRES 4 D 405 LYS LYS ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY
SEQRES 5 D 405 ILE GLY PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU
SEQRES 6 D 405 GLN GLN ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE
SEQRES 7 D 405 ARG GLU MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL
SEQRES 8 D 405 GLY VAL PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS
SEQRES 9 D 405 GLU SER ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR
SEQRES 10 D 405 LYS TRP ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS
SEQRES 11 D 405 GLY LEU LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA
SEQRES 12 D 405 ASN LEU ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP
SEQRES 13 D 405 ALA SER THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP
SEQRES 14 D 405 LEU MET VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE
SEQRES 15 D 405 GLY GLU PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU
SEQRES 16 D 405 GLU VAL GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU
SEQRES 17 D 405 ILE ASP ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG
SEQRES 18 D 405 LYS ARG ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN
SEQRES 19 D 405 VAL LEU GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR
SEQRES 20 D 405 ALA LEU ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS
SEQRES 21 D 405 MET TYR VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP
SEQRES 22 D 405 PRO LYS GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE
SEQRES 23 D 405 GLY ASP ILE LEU SER ASP GLU ALA SER MET ILE THR GLY
SEQRES 24 D 405 SER ILE GLY MET LEU PRO SER ALA SER LEU SER ASP SER
SEQRES 25 D 405 GLY PRO GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO
SEQRES 26 D 405 ASP ILE ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR
SEQRES 27 D 405 ILE LEU SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY
SEQRES 28 D 405 GLU GLU LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU
SEQRES 29 D 405 VAL ALA LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR
SEQRES 30 D 405 SER ALA GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY
SEQRES 31 D 405 GLU GLU VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA
SEQRES 32 D 405 SER VAL
HET ACT A 368 4
HET ACT A 369 4
HET ACT A 370 4
HET ACT A 371 4
HET ACT A 372 4
HET ACT B 368 4
HET ACT B 369 4
HET ACT B 370 4
HET ACT B 371 4
HET ACT B 372 4
HET ACT B 373 4
HET ACT C 368 4
HET ACT D 368 4
HET ACT D 369 4
HET ACT D 370 4
HETNAM ACT ACETATE ION
FORMUL 5 ACT 15(C2 H3 O2 1-)
FORMUL 20 HOH *458(H2 O)
HELIX 1 1 ILE A 15 GLU A 34 1 20
HELIX 2 2 ILE A 45 GLY A 54 1 10
HELIX 3 3 PRO A 58 SER A 68 1 11
HELIX 4 4 GLY A 78 ASP A 82 5 5
HELIX 5 5 GLU A 85 LEU A 88 5 4
HELIX 6 6 ARG A 89 LYS A 102 1 14
HELIX 7 7 LEU A 113 SER A 120 5 8
HELIX 8 8 LYS A 123 GLU A 128 1 6
HELIX 9 9 ALA A 168 LYS A 184 1 17
HELIX 10 10 LEU A 198 ALA A 212 1 15
HELIX 11 11 SER A 213 TYR A 215 5 3
HELIX 12 12 VAL A 225 ASP A 235 1 11
HELIX 13 13 PRO A 236 PHE A 239 5 4
HELIX 14 14 ASN A 245 GLY A 261 1 17
HELIX 15 15 SER A 262 MET A 265 5 4
HELIX 16 16 ALA A 286 ALA A 290 5 5
HELIX 17 17 PRO A 297 GLY A 311 1 15
HELIX 18 18 LYS A 316 ASN A 331 1 16
HELIX 19 19 THR A 335 TYR A 339 5 5
HELIX 20 20 GLY A 347 ASP A 360 1 14
HELIX 21 21 ILE B 15 GLU B 34 1 20
HELIX 22 22 ILE B 45 GLY B 54 1 10
HELIX 23 23 PRO B 58 SER B 68 1 11
HELIX 24 24 GLY B 78 ASP B 82 5 5
HELIX 25 25 GLU B 85 LEU B 88 5 4
HELIX 26 26 ARG B 89 LYS B 102 1 14
HELIX 27 27 LEU B 113 SER B 120 5 8
HELIX 28 28 LYS B 123 GLU B 128 1 6
HELIX 29 29 GLY B 140 PHE B 144 5 5
HELIX 30 30 ALA B 168 LYS B 184 1 17
HELIX 31 31 LEU B 198 ALA B 212 1 15
HELIX 32 32 SER B 213 TYR B 215 5 3
HELIX 33 33 VAL B 225 ASP B 235 1 11
HELIX 34 34 PRO B 236 PHE B 239 5 4
HELIX 35 35 ASN B 245 GLY B 261 1 17
HELIX 36 36 SER B 262 MET B 265 5 4
HELIX 37 37 ALA B 286 ALA B 290 5 5
HELIX 38 38 PRO B 297 GLY B 311 1 15
HELIX 39 39 GLU B 314 ASN B 331 1 18
HELIX 40 40 THR B 335 TYR B 339 5 5
HELIX 41 41 GLY B 347 ASP B 360 1 14
HELIX 42 42 ILE C 15 GLU C 34 1 20
HELIX 43 43 ILE C 45 GLY C 54 1 10
HELIX 44 44 PRO C 58 SER C 68 1 11
HELIX 45 45 GLY C 78 ASN C 83 1 6
HELIX 46 46 GLU C 85 LEU C 88 5 4
HELIX 47 47 ARG C 89 LYS C 102 1 14
HELIX 48 48 LEU C 113 SER C 120 5 8
HELIX 49 49 LYS C 123 GLU C 128 1 6
HELIX 50 50 GLY C 140 PHE C 144 5 5
HELIX 51 51 GLU C 154 GLY C 156 5 3
HELIX 52 52 ALA C 168 LYS C 184 1 17
HELIX 53 53 LEU C 198 ALA C 212 1 15
HELIX 54 54 SER C 213 TYR C 215 5 3
HELIX 55 55 VAL C 225 ASP C 235 1 11
HELIX 56 56 PRO C 236 PHE C 239 5 4
HELIX 57 57 ASN C 245 GLY C 261 1 17
HELIX 58 58 SER C 262 MET C 265 5 4
HELIX 59 59 PRO C 297 GLY C 311 1 15
HELIX 60 60 LYS C 316 ASN C 331 1 16
HELIX 61 61 THR C 335 TYR C 339 5 5
HELIX 62 62 GLY C 347 ASP C 360 1 14
HELIX 63 63 ILE D 15 GLU D 34 1 20
HELIX 64 64 ILE D 45 VAL D 53 1 9
HELIX 65 65 PRO D 58 SER D 68 1 11
HELIX 66 66 GLY D 78 ASN D 83 1 6
HELIX 67 67 GLU D 85 LEU D 88 5 4
HELIX 68 68 ARG D 89 LYS D 102 1 14
HELIX 69 69 LEU D 113 SER D 120 5 8
HELIX 70 70 LYS D 123 GLU D 128 1 6
HELIX 71 71 ALA D 168 LYS D 184 1 17
HELIX 72 72 LEU D 198 ALA D 212 1 15
HELIX 73 73 SER D 213 TYR D 215 5 3
HELIX 74 74 VAL D 225 ASP D 235 1 11
HELIX 75 75 PRO D 236 PHE D 239 5 4
HELIX 76 76 ASN D 245 GLY D 261 1 17
HELIX 77 77 SER D 262 MET D 265 5 4
HELIX 78 78 PRO D 297 GLY D 311 1 15
HELIX 79 79 LYS D 316 ASN D 331 1 16
HELIX 80 80 THR D 335 TYR D 339 5 5
HELIX 81 81 GLY D 347 ASP D 360 1 14
SHEET 1 A10 GLU A 37 GLU A 42 0
SHEET 2 A10 ARG A 4 GLY A 12 1 N TYR A 5 O ASN A 39
SHEET 3 A10 ALA A 70 ALA A 75 1 O GLY A 74 N LEU A 10
SHEET 4 A10 LEU A 278 PRO A 281 1 O PHE A 279 N LEU A 73
SHEET 5 A10 PRO A 267 LEU A 271 -1 N SER A 270 O LEU A 278
SHEET 6 A10 ALA A 105 THR A 111 -1 N LEU A 107 O ALA A 269
SHEET 7 A10 ASP A 131 GLU A 137 -1 O LEU A 132 N ALA A 110
SHEET 8 A10 THR A 241 THR A 244 1 O ILE A 242 N VAL A 135
SHEET 9 A10 LYS A 188 ASP A 193 1 N VAL A 192 O VAL A 243
SHEET 10 A10 GLU A 219 TYR A 224 1 O SER A 221 N SER A 191
SHEET 1 B 4 GLY A 149 THR A 152 0
SHEET 2 B 4 GLU A 158 ALA A 167 -1 O VAL A 159 N LYS A 151
SHEET 3 B 4 GLU B 158 ALA B 167 -1 O TYR B 166 N GLY A 160
SHEET 4 B 4 GLY B 149 THR B 152 -1 N LYS B 151 O VAL B 159
SHEET 1 C 2 PHE A 333 ARG A 334 0
SHEET 2 C 2 LYS A 344 LEU A 345 1 O LYS A 344 N ARG A 334
SHEET 1 D10 GLU B 37 GLU B 42 0
SHEET 2 D10 ARG B 4 GLY B 12 1 N ILE B 7 O ASN B 39
SHEET 3 D10 ALA B 70 ALA B 75 1 O GLY B 74 N LEU B 10
SHEET 4 D10 GLY B 277 PRO B 281 1 O PHE B 279 N LEU B 73
SHEET 5 D10 PRO B 267 LEU B 271 -1 N SER B 270 O LEU B 278
SHEET 6 D10 ALA B 105 THR B 111 -1 N LEU B 107 O ALA B 269
SHEET 7 D10 ASP B 131 GLU B 137 -1 O ARG B 136 N ASN B 106
SHEET 8 D10 THR B 241 THR B 244 1 O ILE B 242 N VAL B 135
SHEET 9 D10 LYS B 188 ASP B 193 1 N CYS B 190 O THR B 241
SHEET 10 D10 GLU B 219 TYR B 224 1 O SER B 221 N SER B 191
SHEET 1 E 2 PHE B 333 ARG B 334 0
SHEET 2 E 2 LYS B 344 LEU B 345 1 O LYS B 344 N ARG B 334
SHEET 1 F10 GLU C 37 GLU C 42 0
SHEET 2 F10 ARG C 4 GLY C 12 1 N LEU C 9 O ARG C 41
SHEET 3 F10 ALA C 70 ALA C 75 1 O LEU C 72 N LEU C 10
SHEET 4 F10 GLY C 277 PRO C 281 1 O PHE C 279 N LEU C 73
SHEET 5 F10 PRO C 267 LEU C 271 -1 N SER C 270 O LEU C 278
SHEET 6 F10 ALA C 105 THR C 111 -1 N LEU C 107 O ALA C 269
SHEET 7 F10 ASP C 131 GLU C 137 -1 O ARG C 136 N ASN C 106
SHEET 8 F10 THR C 241 THR C 244 1 O ILE C 242 N VAL C 135
SHEET 9 F10 LYS C 188 ASP C 193 1 N VAL C 192 O VAL C 243
SHEET 10 F10 GLU C 219 TYR C 224 1 O SER C 221 N SER C 191
SHEET 1 G 4 GLY C 149 THR C 152 0
SHEET 2 G 4 GLU C 158 ALA C 167 -1 O VAL C 159 N LYS C 151
SHEET 3 G 4 GLU D 158 ALA D 167 -1 O TYR D 166 N GLY C 160
SHEET 4 G 4 GLY D 149 THR D 152 -1 N LYS D 151 O VAL D 159
SHEET 1 H 2 PHE C 333 ARG C 334 0
SHEET 2 H 2 LYS C 344 LEU C 345 1 O LYS C 344 N ARG C 334
SHEET 1 I10 GLU D 37 GLU D 42 0
SHEET 2 I10 ARG D 4 GLY D 12 1 N TYR D 5 O ASN D 39
SHEET 3 I10 ALA D 70 ALA D 75 1 O LEU D 72 N LEU D 10
SHEET 4 I10 GLY D 277 PRO D 281 1 O PHE D 279 N LEU D 73
SHEET 5 I10 PRO D 267 LEU D 271 -1 N SER D 270 O LEU D 278
SHEET 6 I10 ALA D 105 THR D 111 -1 N LEU D 107 O ALA D 269
SHEET 7 I10 ASP D 131 GLU D 137 -1 O LEU D 132 N ALA D 110
SHEET 8 I10 THR D 241 THR D 244 1 O ILE D 242 N VAL D 135
SHEET 9 I10 LYS D 188 ASP D 193 1 N VAL D 192 O VAL D 243
SHEET 10 I10 GLU D 219 TYR D 224 1 O SER D 221 N SER D 191
SHEET 1 J 2 PHE D 333 ARG D 334 0
SHEET 2 J 2 LYS D 344 LEU D 345 1 O LYS D 344 N ARG D 334
CISPEP 1 GLU A 146 PRO A 147 0 -0.54
CISPEP 2 GLU B 146 PRO B 147 0 1.12
CISPEP 3 GLU C 146 PRO C 147 0 0.36
CISPEP 4 GLU D 146 PRO D 147 0 0.45
SITE 1 AC1 3 LYS A 151 PHE A 161 GLU B 146
SITE 1 AC2 2 HIS A 169 ARG A 173
SITE 1 AC3 4 GLU A 91 ARG A 98 ARG A 108 ARG A 136
SITE 1 AC4 2 ASP A 235 GLN A 238
SITE 1 AC5 4 ILE A 15 ASN A 296 ASP A 337 HOH A 487
SITE 1 AC6 2 HIS B 169 ARG B 173
SITE 1 AC7 2 ASP B 235 GLN B 238
SITE 1 AC8 2 ASP B 254 ILE B 282
SITE 1 AC9 2 ASN B 296 ASP B 337
SITE 1 BC1 1 ARG B 207
SITE 1 BC2 4 GLU B 91 ARG B 98 ARG B 108 ARG B 136
SITE 1 BC3 3 ARG C 98 ARG C 108 ARG C 136
SITE 1 BC4 4 GLU D 91 ARG D 98 ARG D 108 ARG D 136
SITE 1 BC5 3 ASP D 235 LYS D 237 GLN D 238
SITE 1 BC6 2 ARG D 108 ASP D 254
CRYST1 76.812 211.016 76.903 90.00 90.15 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 0.013019 0.000000 0.000035 0.00000
SCALE2 0.000000 0.004739 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013003 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
