HEADER TRANSFERASE 27-NOV-17 6BQ7
TITLE CRYSTAL STRUCTURE OF MEDICAGO TRUNCATULA THERMOSPERMINE SYNTHASE
TITLE 2 (MTTSPS) IN COMPLEX WITH SPERMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSPERMINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEDICAGO TRUNCATULA;
SOURCE 3 ORGANISM_TAXID: 3880;
SOURCE 4 TISSUE: LEAVES;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS POLYAMINE BIOSYNTHESIS, TETRAAMINE, THERMOSPERMINE, SPERMIDINE,
KEYWDS 2 AMINOPROPYL TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SEKULA,Z.DAUTER
REVDAT 5 04-OCT-23 6BQ7 1 REMARK
REVDAT 4 23-MAR-22 6BQ7 1 REMARK
REVDAT 3 02-MAY-18 6BQ7 1 JRNL
REVDAT 2 07-MAR-18 6BQ7 1 JRNL
REVDAT 1 28-FEB-18 6BQ7 0
JRNL AUTH B.SEKULA,Z.DAUTER
JRNL TITL CRYSTAL STRUCTURE OF THERMOSPERMINE SYNTHASE FROMMEDICAGO
JRNL TITL 2 TRUNCATULAAND SUBSTRATE DISCRIMINATORY FEATURES OF PLANT
JRNL TITL 3 AMINOPROPYLTRANSFERASES.
JRNL REF BIOCHEM. J. V. 475 787 2018
JRNL REFN ESSN 1470-8728
JRNL PMID 29367265
JRNL DOI 10.1042/BCJ20170900
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 39438
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1026
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 39.2512 - 3.7270 1.00 5805 155 0.1488 0.2068
REMARK 3 2 3.7270 - 2.9585 1.00 5546 148 0.1893 0.2453
REMARK 3 3 2.9585 - 2.5846 1.00 5469 146 0.2233 0.2837
REMARK 3 4 2.5846 - 2.3483 1.00 5449 146 0.2349 0.2934
REMARK 3 5 2.3483 - 2.1800 1.00 5390 144 0.2494 0.2921
REMARK 3 6 2.1800 - 2.0515 1.00 5399 145 0.2712 0.3312
REMARK 3 7 2.0515 - 1.9488 0.99 5354 142 0.3062 0.3240
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.860
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) : 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 : 0.007 4813
REMARK 3 ANGLE : 0.915 6517
REMARK 3 CHIRALITY : 0.056 720
REMARK 3 PLANARITY : 0.006 832
REMARK 3 DIHEDRAL : 7.870 3998
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 24 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6985 7.7788 5.5859
REMARK 3 T TENSOR
REMARK 3 T11: 0.4094 T22: 0.4499
REMARK 3 T33: 0.3648 T12: 0.0645
REMARK 3 T13: 0.0174 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 1.4935 L22: 6.4926
REMARK 3 L33: 3.2150 L12: 1.3113
REMARK 3 L13: -0.3272 L23: -0.2157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: 0.3477 S13: 0.1936
REMARK 3 S21: -0.7042 S22: -0.0920 S23: 0.1709
REMARK 3 S31: 0.0286 S32: -0.3625 S33: 0.0053
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 71 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9395 -8.0922 22.2027
REMARK 3 T TENSOR
REMARK 3 T11: 0.3350 T22: 0.3289
REMARK 3 T33: 0.3649 T12: -0.0112
REMARK 3 T13: -0.0409 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.8555 L22: 3.7595
REMARK 3 L33: 5.1967 L12: 0.5345
REMARK 3 L13: 0.1906 L23: 0.1788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0401 S12: -0.0143 S13: -0.3427
REMARK 3 S21: 0.1791 S22: 0.0598 S23: -0.1644
REMARK 3 S31: 0.6840 S32: -0.1665 S33: -0.1049
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5969 -6.6129 21.2527
REMARK 3 T TENSOR
REMARK 3 T11: 0.5523 T22: 0.9302
REMARK 3 T33: 0.5644 T12: -0.1106
REMARK 3 T13: -0.1488 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 7.1025 L22: 7.3581
REMARK 3 L33: 3.7140 L12: 1.8248
REMARK 3 L13: -1.8271 L23: 0.2049
REMARK 3 S TENSOR
REMARK 3 S11: -0.1243 S12: 0.5212 S13: -0.1844
REMARK 3 S21: -0.6916 S22: -0.0110 S23: 1.3124
REMARK 3 S31: 0.3672 S32: -1.6999 S33: -0.0841
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 315 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6633 2.9849 31.4912
REMARK 3 T TENSOR
REMARK 3 T11: 0.3347 T22: 0.5497
REMARK 3 T33: 0.3061 T12: 0.0104
REMARK 3 T13: 0.0261 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.3375 L22: 4.5685
REMARK 3 L33: 3.8705 L12: -0.1378
REMARK 3 L13: 0.2631 L23: -0.4371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.2299 S13: -0.0824
REMARK 3 S21: 0.4979 S22: 0.0761 S23: 0.2823
REMARK 3 S31: 0.0991 S32: -0.7405 S33: -0.0597
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8301 32.9026 20.8529
REMARK 3 T TENSOR
REMARK 3 T11: 0.6498 T22: 0.5582
REMARK 3 T33: 0.4179 T12: 0.3070
REMARK 3 T13: -0.0302 T23: -0.0675
REMARK 3 L TENSOR
REMARK 3 L11: 1.7731 L22: 3.0333
REMARK 3 L33: 3.3056 L12: -0.4294
REMARK 3 L13: 0.8107 L23: -0.3097
REMARK 3 S TENSOR
REMARK 3 S11: -0.4201 S12: -0.2391 S13: 0.1311
REMARK 3 S21: 0.5804 S22: 0.4323 S23: 0.0514
REMARK 3 S31: -0.7702 S32: -0.4607 S33: -0.0069
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 132 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4966 43.1266 26.3676
REMARK 3 T TENSOR
REMARK 3 T11: 1.0910 T22: 0.5770
REMARK 3 T33: 0.6197 T12: 0.3638
REMARK 3 T13: -0.1077 T23: -0.0947
REMARK 3 L TENSOR
REMARK 3 L11: 2.0449 L22: 3.3883
REMARK 3 L33: 2.7453 L12: 0.1651
REMARK 3 L13: 1.4210 L23: -0.1078
REMARK 3 S TENSOR
REMARK 3 S11: -0.2980 S12: 0.0192 S13: 0.4855
REMARK 3 S21: 0.4581 S22: 0.1737 S23: -0.4415
REMARK 3 S31: -1.1343 S32: -0.3785 S33: 0.0038
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7954 28.8277 34.7055
REMARK 3 T TENSOR
REMARK 3 T11: 0.8004 T22: 0.5321
REMARK 3 T33: 0.4173 T12: 0.3288
REMARK 3 T13: -0.1864 T23: -0.1295
REMARK 3 L TENSOR
REMARK 3 L11: 1.1319 L22: 4.6982
REMARK 3 L33: 1.9248 L12: -0.1600
REMARK 3 L13: 0.6770 L23: 0.2452
REMARK 3 S TENSOR
REMARK 3 S11: -0.3825 S12: -0.4664 S13: 0.0854
REMARK 3 S21: 1.0084 S22: 0.3334 S23: -0.6736
REMARK 3 S31: -0.8243 S32: -0.6817 S33: -0.0721
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0151 22.7655 33.3877
REMARK 3 T TENSOR
REMARK 3 T11: 0.6027 T22: 0.4701
REMARK 3 T33: 0.5186 T12: 0.2224
REMARK 3 T13: -0.1094 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.6069 L22: 4.5739
REMARK 3 L33: 4.2338 L12: -0.3866
REMARK 3 L13: 0.2335 L23: 0.5874
REMARK 3 S TENSOR
REMARK 3 S11: -0.2632 S12: -0.1055 S13: 0.6251
REMARK 3 S21: 0.8268 S22: 0.3908 S23: -0.5416
REMARK 3 S31: -0.5973 S32: -0.7042 S33: -0.1411
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 6BQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-17
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 : 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) : 0.979
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1, 2016
REMARK 200 DATA SCALING SOFTWARE : XDS NOV 1, 2016
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39529
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 39.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 207.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.77900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 6BQ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 0.1 M MAGNESIUM CHLORIDE,
REMARK 280 0.1 M BIS-TRIS PROPANE BUFFER CRYO 33% PEG400, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 81.76600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.98100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.98100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 122.64900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.98100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.98100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.88300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.98100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.98100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 122.64900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.98100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.98100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.88300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 81.76600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 VAL A 4
REMARK 465 ALA A 5
REMARK 465 TYR A 6
REMARK 465 THR A 7
REMARK 465 ASN A 8
REMARK 465 GLY A 9
REMARK 465 ASN A 10
REMARK 465 GLY A 11
REMARK 465 ASN A 12
REMARK 465 ASP A 13
REMARK 465 LYS A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 SER A 17
REMARK 465 PRO A 18
REMARK 465 PRO A 19
REMARK 465 ASN A 20
REMARK 465 GLY A 21
REMARK 465 TYR A 22
REMARK 465 ARG A 23
REMARK 465 GLY A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 ARG A 319
REMARK 465 PHE A 320
REMARK 465 ILE A 321
REMARK 465 TYR A 322
REMARK 465 GLY A 323
REMARK 465 HIS A 324
REMARK 465 GLY A 325
REMARK 465 LYS A 326
REMARK 465 ASN A 327
REMARK 465 ALA A 328
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLU B 3
REMARK 465 VAL B 4
REMARK 465 ALA B 5
REMARK 465 TYR B 6
REMARK 465 THR B 7
REMARK 465 ASN B 8
REMARK 465 GLY B 9
REMARK 465 ASN B 10
REMARK 465 GLY B 11
REMARK 465 ASN B 12
REMARK 465 ASP B 13
REMARK 465 LYS B 14
REMARK 465 SER B 15
REMARK 465 HIS B 16
REMARK 465 SER B 17
REMARK 465 PRO B 18
REMARK 465 PRO B 19
REMARK 465 ASN B 20
REMARK 465 GLY B 21
REMARK 465 TYR B 22
REMARK 465 ARG B 23
REMARK 465 GLU B 315
REMARK 465 GLY B 316
REMARK 465 ALA B 317
REMARK 465 ALA B 318
REMARK 465 ARG B 319
REMARK 465 PHE B 320
REMARK 465 ILE B 321
REMARK 465 TYR B 322
REMARK 465 GLY B 323
REMARK 465 HIS B 324
REMARK 465 GLY B 325
REMARK 465 LYS B 326
REMARK 465 ASN B 327
REMARK 465 ALA B 328
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 MET A 98 86.99 -167.57
REMARK 500 ASP A 266 74.02 -151.77
REMARK 500 GLU A 282 168.82 77.50
REMARK 500 ALA B 50 148.32 -171.38
REMARK 500 MET B 98 73.63 -164.16
REMARK 500 LYS B 124 114.36 -173.22
REMARK 500 HIS B 150 43.68 -94.20
REMARK 500 VAL B 226 -25.48 -142.16
REMARK 500 VAL B 237 -39.32 -141.32
REMARK 500 LEU B 265 56.16 -118.20
REMARK 500 GLU B 282 163.49 64.39
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 SPD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD B 401
DBREF 6BQ7 A 1 328 UNP G7K2D1 G7K2D1_MEDTR 1 328
DBREF 6BQ7 B 1 328 UNP G7K2D1 G7K2D1_MEDTR 1 328
SEQADV 6BQ7 SER A -2 UNP G7K2D1 EXPRESSION TAG
SEQADV 6BQ7 ASN A -1 UNP G7K2D1 EXPRESSION TAG
SEQADV 6BQ7 ALA A 0 UNP G7K2D1 EXPRESSION TAG
SEQADV 6BQ7 SER B -2 UNP G7K2D1 EXPRESSION TAG
SEQADV 6BQ7 ASN B -1 UNP G7K2D1 EXPRESSION TAG
SEQADV 6BQ7 ALA B 0 UNP G7K2D1 EXPRESSION TAG
SEQRES 1 A 331 SER ASN ALA MET GLY GLU VAL ALA TYR THR ASN GLY ASN
SEQRES 2 A 331 GLY ASN ASP LYS SER HIS SER PRO PRO ASN GLY TYR ARG
SEQRES 3 A 331 LYS SER CYS TRP TYR GLU GLU GLU ILE GLU GLU ASN LEU
SEQRES 4 A 331 ARG TRP CYS PHE ALA LEU ASN SER ILE LEU HIS THR GLY
SEQRES 5 A 331 ALA SER GLN TYR GLN ASP ILE ALA LEU LEU ASP THR LYS
SEQRES 6 A 331 PRO PHE GLY LYS ALA LEU VAL LEU ASP GLY LYS LEU GLN
SEQRES 7 A 331 SER ALA GLU THR ASP GLU PHE ILE TYR HIS GLU CYS LEU
SEQRES 8 A 331 VAL HIS PRO ALA LEU LEU HIS HIS PRO MET PRO LYS ASN
SEQRES 9 A 331 VAL PHE ILE MET GLY GLY GLY GLU GLY SER THR ALA ARG
SEQRES 10 A 331 GLU LEU LEU ARG HIS LYS THR ILE ASP LYS VAL VAL MET
SEQRES 11 A 331 CYS ASP ILE ASP GLU GLU VAL VAL GLU PHE CYS LYS SER
SEQRES 12 A 331 TYR LEU VAL VAL ASN LYS GLU ALA PHE HIS ASP SER ARG
SEQRES 13 A 331 LEU GLU VAL VAL ILE ASN ASP ALA LYS ALA GLU LEU GLU
SEQRES 14 A 331 GLY LYS GLU GLU LYS TYR ASP VAL ILE VAL GLY ASP LEU
SEQRES 15 A 331 ALA ASP PRO ILE GLU GLY GLY PRO CYS TYR LYS LEU TYR
SEQRES 16 A 331 THR LYS ASP PHE TYR GLU LEU THR LEU LYS PRO LYS LEU
SEQRES 17 A 331 LYS LYS GLY GLY ILE PHE VAL THR GLN ALA GLY PRO ALA
SEQRES 18 A 331 GLY ILE PHE SER HIS THR GLU VAL PHE SER CYS ILE TYR
SEQRES 19 A 331 ASN THR LEU ARG GLN VAL PHE LYS TYR VAL VAL PRO TYR
SEQRES 20 A 331 SER ALA HIS ILE PRO SER TYR ALA ASP ILE TRP GLY TRP
SEQRES 21 A 331 VAL LEU ALA SER ASP SER PRO LEU ASP LEU SER ALA GLU
SEQRES 22 A 331 GLU LEU ASP ILE ARG MET ARG GLN ARG ILE ILE GLU GLU
SEQRES 23 A 331 ASN ARG TYR LEU ASP GLY LYS THR PHE VAL SER SER SER
SEQRES 24 A 331 THR LEU SER LYS ALA VAL ARG ASN SER LEU ASN ASN GLU
SEQRES 25 A 331 THR HIS VAL TYR THR GLU GLY ALA ALA ARG PHE ILE TYR
SEQRES 26 A 331 GLY HIS GLY LYS ASN ALA
SEQRES 1 B 331 SER ASN ALA MET GLY GLU VAL ALA TYR THR ASN GLY ASN
SEQRES 2 B 331 GLY ASN ASP LYS SER HIS SER PRO PRO ASN GLY TYR ARG
SEQRES 3 B 331 LYS SER CYS TRP TYR GLU GLU GLU ILE GLU GLU ASN LEU
SEQRES 4 B 331 ARG TRP CYS PHE ALA LEU ASN SER ILE LEU HIS THR GLY
SEQRES 5 B 331 ALA SER GLN TYR GLN ASP ILE ALA LEU LEU ASP THR LYS
SEQRES 6 B 331 PRO PHE GLY LYS ALA LEU VAL LEU ASP GLY LYS LEU GLN
SEQRES 7 B 331 SER ALA GLU THR ASP GLU PHE ILE TYR HIS GLU CYS LEU
SEQRES 8 B 331 VAL HIS PRO ALA LEU LEU HIS HIS PRO MET PRO LYS ASN
SEQRES 9 B 331 VAL PHE ILE MET GLY GLY GLY GLU GLY SER THR ALA ARG
SEQRES 10 B 331 GLU LEU LEU ARG HIS LYS THR ILE ASP LYS VAL VAL MET
SEQRES 11 B 331 CYS ASP ILE ASP GLU GLU VAL VAL GLU PHE CYS LYS SER
SEQRES 12 B 331 TYR LEU VAL VAL ASN LYS GLU ALA PHE HIS ASP SER ARG
SEQRES 13 B 331 LEU GLU VAL VAL ILE ASN ASP ALA LYS ALA GLU LEU GLU
SEQRES 14 B 331 GLY LYS GLU GLU LYS TYR ASP VAL ILE VAL GLY ASP LEU
SEQRES 15 B 331 ALA ASP PRO ILE GLU GLY GLY PRO CYS TYR LYS LEU TYR
SEQRES 16 B 331 THR LYS ASP PHE TYR GLU LEU THR LEU LYS PRO LYS LEU
SEQRES 17 B 331 LYS LYS GLY GLY ILE PHE VAL THR GLN ALA GLY PRO ALA
SEQRES 18 B 331 GLY ILE PHE SER HIS THR GLU VAL PHE SER CYS ILE TYR
SEQRES 19 B 331 ASN THR LEU ARG GLN VAL PHE LYS TYR VAL VAL PRO TYR
SEQRES 20 B 331 SER ALA HIS ILE PRO SER TYR ALA ASP ILE TRP GLY TRP
SEQRES 21 B 331 VAL LEU ALA SER ASP SER PRO LEU ASP LEU SER ALA GLU
SEQRES 22 B 331 GLU LEU ASP ILE ARG MET ARG GLN ARG ILE ILE GLU GLU
SEQRES 23 B 331 ASN ARG TYR LEU ASP GLY LYS THR PHE VAL SER SER SER
SEQRES 24 B 331 THR LEU SER LYS ALA VAL ARG ASN SER LEU ASN ASN GLU
SEQRES 25 B 331 THR HIS VAL TYR THR GLU GLY ALA ALA ARG PHE ILE TYR
SEQRES 26 B 331 GLY HIS GLY LYS ASN ALA
HET SPD A 401 10
HET SPD B 401 10
HETNAM SPD SPERMIDINE
HETSYN SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)
FORMUL 3 SPD 2(C7 H19 N3)
FORMUL 5 HOH *113(H2 O)
HELIX 1 AA1 ASP A 80 HIS A 96 1 17
HELIX 2 AA2 GLY A 110 LEU A 117 1 8
HELIX 3 AA3 ASP A 131 LEU A 142 1 12
HELIX 4 AA4 ASN A 145 HIS A 150 1 6
HELIX 5 AA5 ASP A 160 LYS A 168 1 9
HELIX 6 AA6 CYS A 188 TYR A 192 5 5
HELIX 7 AA7 THR A 193 THR A 200 1 8
HELIX 8 AA8 LEU A 201 PRO A 203 5 3
HELIX 9 AA9 PHE A 221 GLU A 225 5 5
HELIX 10 AB1 VAL A 226 GLN A 236 1 11
HELIX 11 AB2 PRO A 249 ALA A 252 5 4
HELIX 12 AB3 SER A 268 ILE A 280 1 13
HELIX 13 AB4 ASP A 288 SER A 296 1 9
HELIX 14 AB5 SER A 299 ASN A 308 1 10
HELIX 15 AB6 ASP B 80 HIS B 95 1 16
HELIX 16 AB7 GLY B 110 ARG B 118 1 9
HELIX 17 AB8 ASP B 131 LEU B 142 1 12
HELIX 18 AB9 ASN B 145 HIS B 150 1 6
HELIX 19 AC1 ASP B 160 LYS B 168 1 9
HELIX 20 AC2 CYS B 188 TYR B 192 5 5
HELIX 21 AC3 THR B 193 THR B 200 1 8
HELIX 22 AC4 LEU B 201 PRO B 203 5 3
HELIX 23 AC5 PHE B 221 GLU B 225 5 5
HELIX 24 AC6 VAL B 226 GLN B 236 1 11
HELIX 25 AC7 PRO B 249 ALA B 252 5 4
HELIX 26 AC8 SER B 268 ILE B 280 1 13
HELIX 27 AC9 ASP B 288 SER B 296 1 9
HELIX 28 AD1 SER B 299 ASN B 308 1 10
SHEET 1 AA1 4 TRP A 27 GLU A 33 0
SHEET 2 AA1 4 LEU A 36 ALA A 50 -1 O PHE A 40 N TYR A 28
SHEET 3 AA1 4 LEU B 36 ALA B 50 -1 O CYS B 39 N ARG A 37
SHEET 4 AA1 4 TRP B 27 GLU B 33 -1 N GLU B 30 O TRP B 38
SHEET 1 AA2 8 LYS A 73 ALA A 77 0
SHEET 2 AA2 8 GLY A 65 LEU A 70 -1 N LEU A 68 O GLN A 75
SHEET 3 AA2 8 ASP A 55 THR A 61 -1 N LEU A 59 O ALA A 67
SHEET 4 AA2 8 LEU A 36 ALA A 50 -1 N ASN A 43 O ASP A 60
SHEET 5 AA2 8 LEU B 36 ALA B 50 -1 O CYS B 39 N ARG A 37
SHEET 6 AA2 8 ASP B 55 THR B 61 -1 O ASP B 60 N ASN B 43
SHEET 7 AA2 8 GLY B 65 LEU B 70 -1 O ALA B 67 N LEU B 59
SHEET 8 AA2 8 LYS B 73 ALA B 77 -1 O GLN B 75 N LEU B 68
SHEET 1 AA3 7 LEU A 154 ILE A 158 0
SHEET 2 AA3 7 LYS A 124 ASP A 129 1 N MET A 127 O VAL A 157
SHEET 3 AA3 7 ASN A 101 GLY A 106 1 N GLY A 106 O CYS A 128
SHEET 4 AA3 7 TYR A 172 ASP A 178 1 O VAL A 176 N MET A 105
SHEET 5 AA3 7 LEU A 205 PRO A 217 1 O VAL A 212 N GLY A 177
SHEET 6 AA3 7 ASP A 253 SER A 261 -1 O GLY A 256 N ALA A 215
SHEET 7 AA3 7 TYR A 240 ILE A 248 -1 N VAL A 242 O LEU A 259
SHEET 1 AA4 7 LEU B 154 ILE B 158 0
SHEET 2 AA4 7 LYS B 124 ASP B 129 1 N MET B 127 O VAL B 157
SHEET 3 AA4 7 ASN B 101 GLY B 106 1 N ILE B 104 O VAL B 126
SHEET 4 AA4 7 TYR B 172 ASP B 178 1 O ASP B 178 N MET B 105
SHEET 5 AA4 7 LEU B 205 PRO B 217 1 O VAL B 212 N GLY B 177
SHEET 6 AA4 7 ASP B 253 SER B 261 -1 O ALA B 260 N PHE B 211
SHEET 7 AA4 7 TYR B 240 ILE B 248 -1 N TYR B 240 O SER B 261
SITE 1 AC1 7 GLU A 30 LEU A 74 GLN A 75 ASP A 178
SITE 2 AC1 7 LEU A 179 TYR A 251 TRP A 255
SITE 1 AC2 9 GLU B 30 LEU B 74 GLN B 75 TYR B 84
SITE 2 AC2 9 ASP B 178 TYR B 251 TRP B 255 HOH B 510
SITE 3 AC2 9 HOH B 513
CRYST1 79.962 79.962 163.532 90.00 90.00 90.00 P 43 21 2 16
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 0.012506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006115 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
