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HEADER SIGNALING PROTEIN 01-NOV-13 4NFU
TITLE STRUCTURE OF THE CENTRAL PLANT IMMUNITY SIGNALING NODE EDS1 IN COMPLEX
TITLE 2 WITH ITS INTERACTION PARTNER SAG101
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EDS1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENHANCED DISEASE SUSCEPTIBILITY 1;
COMPND 5 EC: 3.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SENESCENCE-ASSOCIATED CARBOXYLESTERASE 101;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: SENESCENCE-ASSOCIATED PROTEIN 101, SAG101;
COMPND 11 EC: 3.1.1.1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: EDS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 13 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 14 ORGANISM_TAXID: 3702;
SOURCE 15 GENE: AT5G14930, F2G14.50, SAG101;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET-1
KEYWDS ALPHA/BETA HYDROLASE FOLD, INNATE IMMUNITY, PATHOGEN DEFENSE,
KEYWDS 2 PHYTOALEXIN DEFICIENT 4, PAD4, NUCLEUS, HYDROLASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,K.NIEFIND,J.E.PARKER
REVDAT 1 11-DEC-13 4NFU 0
JRNL AUTH S.WAGNER,J.STUTTMANN,S.RIETZ,R.GUEROIS,E.BRUNSTEIN,J.BAUTOR,
JRNL AUTH 2 K.NIEFIND,J.E.PARKER
JRNL TITL STRUCTURAL BASIS FOR SIGNALING BY EXCLUSIVE EDS1 HETEROMERIC
JRNL TITL 2 COMPLEXES WITH SAG101 OR PAD4 IN PLANT INNATE IMMUNITY.
JRNL REF CELL HOST MICROBE V. 14 1 2013
JRNL REFN ISSN 1931-3128
JRNL DOI 10.1016/J.CHOM.2013.11.006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.WAGNER,S.RIETZ,J.E.PARKER,K.NIEFIND
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 1 TITL 2 ARABIDOPSIS THALIANA EDS1, A KEY COMPONENT OF PLANT
REMARK 1 TITL 3 IMMUNITY, IN COMPLEX WITH ITS SIGNALLING PARTNER SAG101.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 67 245 2011
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 21301097
REMARK 1 DOI 10.1107/S1744309110051249
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 78844
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) : 0.176
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1567
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 34.2824 - 4.9106 1.00 7568 148 0.1556 0.1512
REMARK 3 2 4.9106 - 3.8995 1.00 7281 166 0.1441 0.1486
REMARK 3 3 3.8995 - 3.4071 1.00 7263 136 0.1668 0.2112
REMARK 3 4 3.4071 - 3.0958 1.00 7212 159 0.1990 0.2274
REMARK 3 5 3.0958 - 2.8740 1.00 7195 158 0.1973 0.2397
REMARK 3 6 2.8740 - 2.7046 1.00 7205 115 0.1990 0.2238
REMARK 3 7 2.7046 - 2.5692 1.00 7146 144 0.2028 0.2513
REMARK 3 8 2.5692 - 2.4574 1.00 7151 136 0.2079 0.2352
REMARK 3 9 2.4574 - 2.3629 0.99 7068 144 0.2123 0.2503
REMARK 3 10 2.3629 - 2.2813 0.90 6439 140 0.2393 0.3086
REMARK 3 11 2.2813 - 2.2100 0.81 5749 121 0.2769 0.3056
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.002 9544
REMARK 3 ANGLE : 0.623 12879
REMARK 3 CHIRALITY : 0.023 1398
REMARK 3 PLANARITY : 0.003 1643
REMARK 3 DIHEDRAL : 11.229 3592
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 2 through 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4256 6.1975 69.2793
REMARK 3 T TENSOR
REMARK 3 T11: 0.3762 T22: 0.3186
REMARK 3 T33: 0.3499 T12: 0.0243
REMARK 3 T13: -0.0441 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 4.0166 L22: 2.5322
REMARK 3 L33: 5.9564 L12: -0.0011
REMARK 3 L13: -1.8209 L23: 0.7989
REMARK 3 S TENSOR
REMARK 3 S11: 0.0635 S12: -0.2437 S13: -0.1219
REMARK 3 S21: 0.2926 S22: 0.1015 S23: -0.0362
REMARK 3 S31: 0.3405 S32: 0.0469 S33: -0.1020
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 71 through 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4765 8.1981 61.7083
REMARK 3 T TENSOR
REMARK 3 T11: 0.2773 T22: 0.2704
REMARK 3 T33: 0.3433 T12: 0.0167
REMARK 3 T13: 0.0119 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 2.2990 L22: 2.3156
REMARK 3 L33: 4.8630 L12: 0.2085
REMARK 3 L13: 0.3208 L23: -0.2575
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: 0.0530 S13: -0.0430
REMARK 3 S21: 0.0276 S22: 0.2080 S23: 0.1846
REMARK 3 S31: 0.1233 S32: -0.3215 S33: -0.2376
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 185 through 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.0137 16.7361 66.5128
REMARK 3 T TENSOR
REMARK 3 T11: 0.3721 T22: 0.6507
REMARK 3 T33: 0.4228 T12: -0.0528
REMARK 3 T13: -0.0469 T23: -0.0846
REMARK 3 L TENSOR
REMARK 3 L11: 2.3997 L22: 2.5070
REMARK 3 L33: 2.3789 L12: 0.4948
REMARK 3 L13: -0.9240 L23: -0.2371
REMARK 3 S TENSOR
REMARK 3 S11: 0.0561 S12: -0.4200 S13: -0.0034
REMARK 3 S21: 0.3627 S22: 0.0580 S23: -0.4192
REMARK 3 S31: -0.2378 S32: 0.7366 S33: -0.0663
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 338 through 380 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8747 32.8375 55.2166
REMARK 3 T TENSOR
REMARK 3 T11: 0.8260 T22: 0.4902
REMARK 3 T33: 0.5989 T12: -0.1114
REMARK 3 T13: 0.0216 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 5.2735 L22: 0.0345
REMARK 3 L33: 5.7419 L12: 0.3086
REMARK 3 L13: 5.1253 L23: 0.4004
REMARK 3 S TENSOR
REMARK 3 S11: -0.2299 S12: -0.2239 S13: 0.8029
REMARK 3 S21: 0.0201 S22: -0.0977 S23: 0.0078
REMARK 3 S31: -1.0175 S32: -0.0337 S33: 0.5777
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 381 through 524 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6763 18.7293 28.6571
REMARK 3 T TENSOR
REMARK 3 T11: 0.3411 T22: 0.4391
REMARK 3 T33: 0.3437 T12: -0.0498
REMARK 3 T13: -0.0303 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 1.5154 L22: 1.5108
REMARK 3 L33: 4.0316 L12: 0.3158
REMARK 3 L13: 0.2399 L23: -1.2959
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: 0.1805 S13: -0.0690
REMARK 3 S21: -0.1747 S22: 0.1690 S23: 0.1822
REMARK 3 S31: 0.2607 S32: -0.3802 S33: -0.1346
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 525 through 620 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8864 1.7906 21.2465
REMARK 3 T TENSOR
REMARK 3 T11: 0.8368 T22: 0.6113
REMARK 3 T33: 0.7115 T12: -0.2522
REMARK 3 T13: -0.2151 T23: 0.1049
REMARK 3 L TENSOR
REMARK 3 L11: 3.6206 L22: 2.8671
REMARK 3 L33: 2.7808 L12: 0.3867
REMARK 3 L13: -0.2176 L23: 2.0165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0605 S12: 0.0596 S13: -0.6692
REMARK 3 S21: -0.2830 S22: 0.3245 S23: 0.4342
REMARK 3 S31: 0.9312 S32: -0.4585 S33: -0.3498
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resid -2 through 272 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.9418 20.8056 38.3606
REMARK 3 T TENSOR
REMARK 3 T11: 0.4583 T22: 0.4562
REMARK 3 T33: 0.4372 T12: -0.0156
REMARK 3 T13: -0.1028 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 2.9042 L22: 2.1991
REMARK 3 L33: 4.3791 L12: 0.4274
REMARK 3 L13: -0.3491 L23: 0.4084
REMARK 3 S TENSOR
REMARK 3 S11: 0.2671 S12: -0.2094 S13: -0.3875
REMARK 3 S21: 0.1442 S22: -0.1298 S23: -0.0074
REMARK 3 S31: 0.5044 S32: 0.1344 S33: -0.1187
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resid 273 through 537 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.2530 33.3492 3.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3138 T22: 0.3112
REMARK 3 T33: 0.3397 T12: -0.0046
REMARK 3 T13: -0.0194 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.8609 L22: 0.5615
REMARK 3 L33: 2.8006 L12: -0.1771
REMARK 3 L13: 0.7834 L23: -0.1308
REMARK 3 S TENSOR
REMARK 3 S11: 0.1591 S12: 0.0494 S13: -0.1593
REMARK 3 S21: 0.0099 S22: 0.0164 S23: -0.1546
REMARK 3 S31: 0.0964 S32: 0.0127 S33: -0.1884
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 4NFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083149.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0399, 1.0404, 1.0313, 0.9184
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78935
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.05400
REMARK 200 FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.97200
REMARK 200 R SYM FOR SHELL (I) : 0.97200
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP INTEGRATED INTO AUTO-RICKSHAW (EMBL-HAMBURG)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 5% W/V PEG4000,
REMARK 280 5% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 56.29300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.69300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.82150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.69300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.29300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.82150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 5570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 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 -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 GLN A -1
REMARK 465 ASP A 0
REMARK 465 PRO A 1
REMARK 465 THR A 621
REMARK 465 ASP A 622
REMARK 465 THR A 623
REMARK 465 PRO B 36
REMARK 465 TYR B 37
REMARK 465 SER B 38
REMARK 465 ASN B 39
REMARK 465 HIS B 40
REMARK 465 ASP B 41
REMARK 465 PRO B 42
REMARK 465 GLY B 43
REMARK 465 LEU B 44
REMARK 465 GLN B 45
REMARK 465 VAL B 46
REMARK 465 SER B 47
REMARK 465 LYS B 48
REMARK 465 LYS B 49
REMARK 465 LYS B 50
REMARK 465 LYS B 51
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 A 927 O HOH A 928 1.94
REMARK 500 OE2 GLU B 392 O HOH B 825 2.03
REMARK 500 O HOH B 767 O HOH B 770 2.12
REMARK 500 OE2 GLU A 150 O HOH A 955 2.16
REMARK 500 O HOH A 893 O HOH A 924 2.19
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 ARG A 29 -58.37 61.87
REMARK 500 ASP A 98 119.19 -39.14
REMARK 500 SER A 123 -132.37 57.26
REMARK 500 ASN A 144 77.95 -159.79
REMARK 500 PRO A 145 92.50 -69.69
REMARK 500 VAL A 161 -50.84 -120.30
REMARK 500 SER A 216 35.10 -97.50
REMARK 500 ASN B 34 115.49 -164.52
REMARK 500 SER B 53 66.03 -100.37
REMARK 500 SER B 79 35.01 -93.16
REMARK 500 ALA B 146 -123.93 54.86
REMARK 500 MET B 210 45.08 -107.50
REMARK 500 LEU B 265 43.69 -98.07
REMARK 500 ASP B 267 43.52 -90.76
REMARK 500 ASP B 291 16.83 59.09
REMARK 500 MET B 292 74.04 33.51
REMARK 500 MET B 293 28.87 -71.69
REMARK 500 PHE B 294 -51.66 -125.95
REMARK 500 SER B 333 -8.65 -143.24
REMARK 500 HIS B 343 -63.21 -108.49
REMARK 500 CYS B 429 33.39 -88.09
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 BGC A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 602
DBREF 4NFU A 2 623 UNP Q9XF23 Q9XF23_ARATH 2 623
DBREF 4NFU B 2 537 UNP Q4F883 SG101_ARATH 1 536
SEQADV 4NFU MET A -12 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU GLY A -11 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU SER A -10 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU SER A -9 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -8 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -7 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -6 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -5 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -4 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU HIS A -3 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU SER A -2 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU GLN A -1 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU ASP A 0 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU PRO A 1 UNP Q9XF23 EXPRESSION TAG
SEQADV 4NFU SER B -2 UNP Q4F883 EXPRESSION TAG
SEQADV 4NFU GLN B -1 UNP Q4F883 EXPRESSION TAG
SEQADV 4NFU ASP B 0 UNP Q4F883 EXPRESSION TAG
SEQADV 4NFU PRO B 1 UNP Q4F883 EXPRESSION TAG
SEQRES 1 A 636 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 636 PRO ALA PHE GLU ALA LEU THR GLY ILE ASN GLY ASP LEU
SEQRES 3 A 636 ILE THR ARG SER TRP SER ALA SER LYS GLN ALA TYR LEU
SEQRES 4 A 636 THR GLU ARG TYR HIS LYS GLU GLU ALA GLY ALA VAL VAL
SEQRES 5 A 636 ILE PHE ALA PHE GLN PRO SER PHE SER GLU LYS ASP PHE
SEQRES 6 A 636 PHE ASP PRO ASP ASN LYS SER SER PHE GLY GLU ILE LYS
SEQRES 7 A 636 LEU ASN ARG VAL GLN PHE PRO CYS MET ARG LYS ILE GLY
SEQRES 8 A 636 LYS GLY ASP VAL ALA THR VAL ASN GLU ALA PHE LEU LYS
SEQRES 9 A 636 ASN LEU GLU ALA VAL ILE ASP PRO ARG THR SER PHE GLN
SEQRES 10 A 636 ALA SER VAL GLU MET ALA VAL ARG SER ARG LYS GLN ILE
SEQRES 11 A 636 VAL PHE THR GLY HIS SER SER GLY GLY ALA THR ALA ILE
SEQRES 12 A 636 LEU ALA THR VAL TRP TYR LEU GLU LYS TYR PHE ILE ARG
SEQRES 13 A 636 ASN PRO ASN VAL TYR LEU GLU PRO ARG CYS VAL THR PHE
SEQRES 14 A 636 GLY ALA PRO LEU VAL GLY ASP SER ILE PHE SER HIS ALA
SEQRES 15 A 636 LEU GLY ARG GLU LYS TRP SER ARG PHE PHE VAL ASN PHE
SEQRES 16 A 636 VAL THR ARG PHE ASP ILE VAL PRO ARG ILE THR LEU ALA
SEQRES 17 A 636 ARG LYS ALA SER VAL GLU GLU THR LEU PRO HIS VAL LEU
SEQRES 18 A 636 ALA GLN LEU ASP PRO ARG ASN SER SER VAL GLN GLU SER
SEQRES 19 A 636 GLU GLN ARG ILE THR GLU PHE TYR THR SER VAL MET ARG
SEQRES 20 A 636 ASP THR SER THR VAL ALA ASN GLN ALA VAL CYS GLU LEU
SEQRES 21 A 636 THR GLY SER ALA GLU ALA ILE LEU GLU THR LEU SER SER
SEQRES 22 A 636 PHE LEU GLU LEU SER PRO TYR ARG PRO ALA GLY THR PHE
SEQRES 23 A 636 VAL PHE SER THR GLU LYS ARG LEU VAL ALA VAL ASN ASN
SEQRES 24 A 636 SER ASP ALA ILE LEU GLN MET LEU PHE TYR THR CYS GLN
SEQRES 25 A 636 ALA SER ASP GLU GLN GLU TRP SER LEU ILE PRO PHE ARG
SEQRES 26 A 636 SER ILE ARG ASP HIS HIS SER TYR GLU GLU LEU VAL GLN
SEQRES 27 A 636 SER MET GLY MET LYS LEU PHE ASN HIS LEU ASP GLY GLU
SEQRES 28 A 636 ASN SER ILE GLU SER SER LEU ASN ASP LEU GLY VAL SER
SEQRES 29 A 636 THR ARG GLY ARG GLN TYR VAL GLN ALA ALA LEU GLU GLU
SEQRES 30 A 636 GLU LYS LYS ARG VAL GLU ASN GLN LYS LYS ILE ILE GLN
SEQRES 31 A 636 VAL ILE GLN GLN GLU ARG PHE LEU LYS LYS LEU ALA TRP
SEQRES 32 A 636 ILE GLU ASP GLU TYR LYS PRO LYS CYS GLN ALA HIS LYS
SEQRES 33 A 636 ASN GLY TYR TYR ASP SER PHE LYS VAL SER ASN GLU GLU
SEQRES 34 A 636 ASN ASP PHE LYS ALA ASN VAL LYS ARG ALA GLU LEU ALA
SEQRES 35 A 636 GLY VAL PHE ASP GLU VAL LEU GLY LEU LEU LYS LYS CYS
SEQRES 36 A 636 GLN LEU PRO ASP GLU PHE GLU GLY ASP ILE ASP TRP ILE
SEQRES 37 A 636 LYS LEU ALA THR ARG TYR ARG ARG LEU VAL GLU PRO LEU
SEQRES 38 A 636 ASP ILE ALA ASN TYR HIS ARG HIS LEU LYS ASN GLU ASP
SEQRES 39 A 636 THR GLY PRO TYR MET LYS ARG GLY ARG PRO THR ARG TYR
SEQRES 40 A 636 ILE TYR ALA GLN ARG GLY TYR GLU HIS HIS ILE LEU LYS
SEQRES 41 A 636 PRO ASN GLY MET ILE ALA GLU ASP VAL PHE TRP ASN LYS
SEQRES 42 A 636 VAL ASN GLY LEU ASN LEU GLY LEU GLN LEU GLU GLU ILE
SEQRES 43 A 636 GLN GLU THR LEU LYS ASN SER GLY SER GLU CYS GLY SER
SEQRES 44 A 636 CYS PHE TRP ALA GLU VAL GLU GLU LEU LYS GLY LYS PRO
SEQRES 45 A 636 TYR GLU GLU VAL GLU VAL ARG VAL LYS THR LEU GLU GLY
SEQRES 46 A 636 MET LEU ARG GLU TRP ILE THR ALA GLY GLU VAL ASP GLU
SEQRES 47 A 636 LYS GLU ILE PHE LEU GLU GLY SER THR PHE ARG LYS TRP
SEQRES 48 A 636 TRP ILE THR LEU PRO LYS ASN HIS LYS SER HIS SER PRO
SEQRES 49 A 636 LEU ARG ASP TYR MET MET ASP GLU ILE THR ASP THR
SEQRES 1 B 540 SER GLN ASP PRO GLU SER SER SER SER LEU LYS GLY SER
SEQRES 2 B 540 ALA LEU GLY LYS LEU VAL VAL THR SER GLY LEU LEU HIS
SEQRES 3 B 540 SER SER TRP SER LYS ILE LEU GLU ILE HIS ASN PRO PRO
SEQRES 4 B 540 TYR SER ASN HIS ASP PRO GLY LEU GLN VAL SER LYS LYS
SEQRES 5 B 540 LYS LYS ASP SER GLY LEU GLU PHE GLN ILE HIS ARG GLU
SEQRES 6 B 540 GLU LYS PHE THR LEU VAL VAL PHE SER ALA PRO PRO ILE
SEQRES 7 B 540 CYS ARG SER SER SER SER ASP SER THR LEU LEU HIS VAL
SEQRES 8 B 540 LYS ASP LYS GLU ASN PRO PHE PRO PHE LEU CYS SER GLU
SEQRES 9 B 540 ASN ASN PRO SER PHE SER LEU HIS THR PRO ALA PHE ASN
SEQRES 10 B 540 LEU PHE THR SER ALA SER THR SER LEU THR TYR LEU LYS
SEQRES 11 B 540 SER GLU LEU LEU GLN THR LEU LYS SER GLU LYS PRO VAL
SEQRES 12 B 540 ILE ILE THR GLY ALA ALA LEU GLY GLY SER VAL ALA SER
SEQRES 13 B 540 LEU TYR THR LEU TRP LEU LEU GLU THR ILE GLU PRO THR
SEQRES 14 B 540 LEU LYS ARG PRO LEU CYS ILE THR PHE GLY SER PRO LEU
SEQRES 15 B 540 ILE GLY ASP ALA SER LEU GLN GLN ILE LEU GLU ASN SER
SEQRES 16 B 540 VAL ARG ASN SER CYS PHE LEU HIS VAL VAL SER ALA GLN
SEQRES 17 B 540 THR ARG ILE LYS MET ASP PHE PHE LYS PRO PHE GLY THR
SEQRES 18 B 540 PHE LEU ILE CYS PHE ASP SER GLY CYS VAL CYS ILE GLU
SEQRES 19 B 540 ASP HIS VAL ALA VAL THR GLU LEU LEU ASN GLY VAL HIS
SEQRES 20 B 540 ASP SER GLY LEU VAL ASP TYR SER GLN VAL LEU ASN ARG
SEQRES 21 B 540 LEU ASP GLN SER MET LEU SER LEU ALA ASP SER ARG LEU
SEQRES 22 B 540 ILE PRO GLU ASP VAL ILE LYS GLY ILE GLU LYS ARG ALA
SEQRES 23 B 540 GLU MET LYS ASN LEU ARG PHE ASP MET MET PHE LYS LYS
SEQRES 24 B 540 LEU ASN ASP MET LYS ILE SER MET ALA TYR ILE GLU TRP
SEQRES 25 B 540 TYR LYS LYS LYS CYS LYS GLU VAL LYS ILE GLY TYR TYR
SEQRES 26 B 540 ASP ARG PHE LYS THR GLN LEU ALA PHE PRO SER LYS GLU
SEQRES 27 B 540 PHE ASP ILE ASN ILE LYS ASN HIS HIS LYS SER GLU LEU
SEQRES 28 B 540 ASN ARG PHE TRP LYS SER VAL VAL GLU GLU VAL GLU ARG
SEQRES 29 B 540 ARG PRO GLN SER ASP ALA SER ILE LEU LYS ARG ARG PHE
SEQRES 30 B 540 LEU PHE SER GLY ASN ASN TYR ARG ARG MET ILE GLU PRO
SEQRES 31 B 540 LEU ASP ILE ALA GLU TYR TYR LEU GLU GLY ARG LYS GLU
SEQRES 32 B 540 TYR ARG THR THR GLY ARG SER HIS HIS TYR VAL MET LEU
SEQRES 33 B 540 GLU LYS TRP PHE GLY MET GLU SER ILE LEU ILE GLU LYS
SEQRES 34 B 540 GLU ARG CYS LYS LYS ARG ASP LEU SER ASP LEU LEU THR
SEQRES 35 B 540 PHE ASP SER CYS PHE TRP ALA GLU VAL GLU ASP SER LEU
SEQRES 36 B 540 ILE VAL ILE ASN GLN LEU ASN THR THR VAL GLY MET ARG
SEQRES 37 B 540 ASP ASP VAL ARG GLU VAL LEU THR ARG LYS LEU VAL GLU
SEQRES 38 B 540 PHE GLU GLY TYR VAL TRP GLU ILE ILE THR LYS ARG GLU
SEQRES 39 B 540 VAL SER PRO GLU ILE PHE LEU GLU GLU SER SER PHE MET
SEQRES 40 B 540 LYS TRP TRP LYS GLU TYR LYS LYS ILE LYS GLY PHE ASN
SEQRES 41 B 540 SER SER TYR LEU THR GLU PHE MET ASN THR ARG LYS TYR
SEQRES 42 B 540 GLU SER TYR GLY LYS SER GLN
HET BGC A 701 12
HET IPA A 702 4
HET IPA A 703 4
HET EPE B 601 15
HET IPA B 602 4
HETNAM BGC BETA-D-GLUCOSE
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN IPA 2-PROPANOL
HETSYN EPE HEPES
FORMUL 3 BGC C6 H12 O6
FORMUL 4 IPA 3(C3 H8 O)
FORMUL 6 EPE C8 H18 N2 O4 S
FORMUL 8 HOH *302(H2 O)
HELIX 1 1 PHE A 3 GLY A 8 1 6
HELIX 2 2 ASN A 10 ALA A 24 1 15
HELIX 3 3 TYR A 25 THR A 27 5 3
HELIX 4 4 SER A 48 PHE A 52 5 5
HELIX 5 5 GLU A 87 ASP A 98 1 12
HELIX 6 6 PRO A 99 THR A 101 5 3
HELIX 7 7 SER A 102 SER A 113 1 12
HELIX 8 8 SER A 123 TYR A 140 1 18
HELIX 9 9 PHE A 141 ASN A 144 5 4
HELIX 10 10 ASP A 163 GLU A 173 1 11
HELIX 11 11 TRP A 175 ARG A 177 5 3
HELIX 12 12 ILE A 188 ALA A 195 5 8
HELIX 13 13 THR A 203 ASP A 212 1 10
HELIX 14 14 SER A 221 THR A 248 1 28
HELIX 15 15 ALA A 251 SER A 259 1 9
HELIX 16 16 SER A 260 LEU A 262 5 3
HELIX 17 17 ASN A 286 THR A 297 1 12
HELIX 18 18 LEU A 308 ASP A 316 1 9
HELIX 19 19 SER A 319 SER A 326 1 8
HELIX 20 20 MET A 327 LYS A 330 5 4
HELIX 21 21 ASP A 336 GLU A 338 5 3
HELIX 22 22 ILE A 341 LEU A 348 1 8
HELIX 23 23 SER A 351 GLN A 380 1 30
HELIX 24 24 GLN A 381 GLU A 394 1 14
HELIX 25 25 GLU A 394 HIS A 402 1 9
HELIX 26 26 ASN A 404 SER A 413 1 10
HELIX 27 27 GLU A 415 LYS A 441 1 27
HELIX 28 28 GLU A 447 GLY A 450 5 4
HELIX 29 29 ASP A 451 HIS A 476 1 26
HELIX 30 30 LEU A 477 THR A 482 1 6
HELIX 31 31 PRO A 484 GLY A 489 1 6
HELIX 32 32 PRO A 491 LYS A 507 1 17
HELIX 33 33 PRO A 508 GLY A 510 5 3
HELIX 34 34 ILE A 512 GLY A 523 1 12
HELIX 35 35 GLN A 529 LEU A 537 1 9
HELIX 36 36 SER A 540 SER A 546 5 7
HELIX 37 37 CYS A 547 LYS A 556 1 10
HELIX 38 38 VAL A 563 ALA A 580 1 18
HELIX 39 39 SER A 593 THR A 601 1 9
HELIX 40 40 PRO A 603 HIS A 609 1 7
HELIX 41 41 LEU A 612 MET A 616 5 5
HELIX 42 42 SER B 3 SER B 19 1 17
HELIX 43 43 GLY B 20 ASN B 34 1 15
HELIX 44 44 CYS B 76 SER B 80 5 5
HELIX 45 45 PHE B 95 CYS B 99 5 5
HELIX 46 46 THR B 110 SER B 118 1 9
HELIX 47 47 ALA B 119 SER B 136 1 18
HELIX 48 48 ALA B 146 LEU B 160 1 15
HELIX 49 49 ALA B 183 GLU B 190 1 8
HELIX 50 50 ASN B 191 SER B 196 5 6
HELIX 51 51 ASP B 232 ASN B 241 1 10
HELIX 52 52 ASP B 250 LEU B 263 1 14
HELIX 53 53 PRO B 272 ASN B 287 1 16
HELIX 54 54 PHE B 294 VAL B 317 1 24
HELIX 55 55 GLY B 320 PHE B 331 1 12
HELIX 56 56 LYS B 334 HIS B 343 1 10
HELIX 57 57 HIS B 343 ARG B 362 1 20
HELIX 58 58 PRO B 363 PHE B 374 1 12
HELIX 59 59 PHE B 374 GLU B 396 1 23
HELIX 60 60 GLU B 400 GLY B 405 1 6
HELIX 61 61 SER B 407 GLY B 418 1 12
HELIX 62 62 GLU B 420 CYS B 429 1 10
HELIX 63 63 CYS B 443 THR B 461 1 19
HELIX 64 64 ARG B 465 LYS B 489 1 25
HELIX 65 65 SER B 493 LEU B 498 5 6
HELIX 66 66 SER B 501 GLY B 515 1 15
HELIX 67 67 SER B 519 THR B 527 1 9
HELIX 68 68 ARG B 528 TYR B 533 5 6
SHEET 1 A 8 TYR A 30 ALA A 35 0
SHEET 2 A 8 VAL A 38 PHE A 43 -1 O ALA A 42 N HIS A 31
SHEET 3 A 8 GLN A 116 HIS A 122 1 O VAL A 118 N PHE A 41
SHEET 4 A 8 ARG A 152 PHE A 156 1 O ARG A 152 N PHE A 119
SHEET 5 A 8 PHE A 179 THR A 184 1 O VAL A 180 N CYS A 153
SHEET 6 A 8 THR A 272 SER A 276 1 O VAL A 274 N ASN A 181
SHEET 7 A 8 ARG A 280 VAL A 284 -1 O VAL A 284 N PHE A 273
SHEET 8 A 8 LEU A 331 HIS A 334 1 O LEU A 331 N LEU A 281
SHEET 1 B 2 GLU A 63 LYS A 65 0
SHEET 2 B 2 THR A 84 ASN A 86 -1 O VAL A 85 N ILE A 64
SHEET 1 C 7 GLU B 56 ARG B 61 0
SHEET 2 C 7 THR B 66 SER B 71 -1 O LEU B 67 N HIS B 60
SHEET 3 C 7 VAL B 140 ALA B 145 1 O THR B 143 N PHE B 70
SHEET 4 C 7 LEU B 171 PHE B 175 1 O LEU B 171 N ILE B 142
SHEET 5 C 7 PHE B 198 SER B 203 1 O LEU B 199 N CYS B 172
SHEET 6 C 7 THR B 218 PHE B 223 1 O THR B 218 N HIS B 200
SHEET 7 C 7 GLY B 226 ILE B 230 -1 O GLY B 226 N PHE B 223
SHEET 1 D 2 SER B 83 HIS B 87 0
SHEET 2 D 2 SER B 105 HIS B 109 -1 O PHE B 106 N LEU B 86
SHEET 1 E 2 GLY B 181 ASP B 182 0
SHEET 2 E 2 PHE B 213 LYS B 214 -1 O LYS B 214 N GLY B 181
SITE 1 AC1 7 ASN A 285 ASP A 446 HOH A 835 HOH A 909
SITE 2 AC1 7 HOH A 932 HOH A 934 HOH A 938
SITE 1 AC2 1 TYR A 25
SITE 1 AC3 2 LYS A 487 ARG A 488
SITE 1 AC4 9 GLU B 480 GLY B 481 TRP B 484 TYR B 510
SITE 2 AC4 9 ASN B 517 SER B 518 SER B 519 TYR B 520
SITE 3 AC4 9 LEU B 521
SITE 1 AC5 4 THR B 403 THR B 404 GLY B 405 ARG B 406
CRYST1 112.586 113.643 125.386 90.00 90.00 90.00 P 21 21 21 4
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 0.008882 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007975 0.00000
TER 5025 ILE A 620
TER 9299 GLN B 537
MASTER 446 0 5 68 21 0 8 6 9618 2 39 91
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