HEADER OXIDOREDUCTASE 03-JUN-15 5A3V
TITLE CRYSTAL STRUCTURE OF THE CHLOROPLASTIC GAMMA-KETOL REDUCTASE FROM
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE QUINONE-OXIDOREDUCTASE HOMOLOG, CHLOROPLASTIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GAMMA-KETOL REDUCTASE;
COMPND 5 EC: 1.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 TISSUE: CHLOROPLAST;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, GAMMA-KETOL REDUCTASE, ARABIDOPSIS THALIANA,
KEYWDS 2 CHLOROPLAST, OXYDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAS-Y-MAS,G.CURIEN,C.GIUSTINI,N.ROLLAND,J.L.FERRER,D.COBESSI
REVDAT 4 09-AUG-17 5A3V 1 REMARK
REVDAT 3 05-APR-17 5A3V 1 JRNL
REVDAT 2 22-MAR-17 5A3V 1 JRNL
REVDAT 1 28-SEP-16 5A3V 0
JRNL AUTH S.MAS Y MAS,G.CURIEN,C.GIUSTINI,N.ROLLAND,J.L.FERRER,
JRNL AUTH 2 D.COBESSI
JRNL TITL CRYSTAL STRUCTURE OF THE CHLOROPLASTIC OXOENE REDUCTASE
JRNL TITL 2 CEQORH FROM ARABIDOPSIS THALIANA.
JRNL REF FRONT PLANT SCI V. 8 329 2017
JRNL REFN ESSN 1664-462X
JRNL PMID 28337214
JRNL DOI 10.3389/FPLS.2017.00329
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 28266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1412
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 42.2736 - 5.0392 0.99 2905 154 0.1479 0.1979
REMARK 3 2 5.0392 - 4.0007 1.00 2795 147 0.1314 0.1879
REMARK 3 3 4.0007 - 3.4953 0.99 2738 143 0.1809 0.2502
REMARK 3 4 3.4953 - 3.1758 1.00 2737 144 0.1936 0.2485
REMARK 3 5 3.1758 - 2.9482 1.00 2738 144 0.1979 0.2726
REMARK 3 6 2.9482 - 2.7745 1.00 2717 143 0.2154 0.3057
REMARK 3 7 2.7745 - 2.6355 0.99 2679 140 0.2184 0.3317
REMARK 3 8 2.6355 - 2.5208 0.99 2703 142 0.2040 0.2835
REMARK 3 9 2.5208 - 2.4238 0.95 2580 136 0.2115 0.2636
REMARK 3 10 2.4238 - 2.3402 0.85 2262 119 0.2219 0.3292
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.85
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 : 0.011 4998
REMARK 3 ANGLE : 1.350 6806
REMARK 3 CHIRALITY : 0.047 798
REMARK 3 PLANARITY : 0.006 876
REMARK 3 DIHEDRAL : 14.523 1863
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 4:80)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2130 0.3073 -41.9066
REMARK 3 T TENSOR
REMARK 3 T11: 0.1174 T22: 0.1100
REMARK 3 T33: 0.1264 T12: -0.0307
REMARK 3 T13: 0.0333 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 3.0687 L22: 1.6435
REMARK 3 L33: 1.9462 L12: -0.7612
REMARK 3 L13: 0.2325 L23: -0.3101
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.1260 S13: -0.1887
REMARK 3 S21: -0.1012 S22: 0.0339 S23: 0.1276
REMARK 3 S31: 0.1887 S32: -0.1874 S33: -0.0234
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 81:131)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0965 8.1125 -33.6611
REMARK 3 T TENSOR
REMARK 3 T11: 0.1474 T22: 0.1966
REMARK 3 T33: 0.1524 T12: 0.0101
REMARK 3 T13: 0.0455 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 3.6022 L22: 1.0609
REMARK 3 L33: 3.0526 L12: 0.4731
REMARK 3 L13: 0.6190 L23: -0.4124
REMARK 3 S TENSOR
REMARK 3 S11: -0.0326 S12: -0.3084 S13: 0.0269
REMARK 3 S21: 0.1112 S22: 0.0206 S23: 0.2612
REMARK 3 S31: -0.0419 S32: -0.5121 S33: 0.0015
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 132:299)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6558 -6.8947 -14.8221
REMARK 3 T TENSOR
REMARK 3 T11: 0.1523 T22: 0.1537
REMARK 3 T33: 0.1157 T12: -0.0070
REMARK 3 T13: 0.0239 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.0853 L22: 3.4563
REMARK 3 L33: 1.9752 L12: -0.3391
REMARK 3 L13: 0.7296 L23: -0.6782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: -0.1512 S13: -0.0674
REMARK 3 S21: 0.3601 S22: 0.0322 S23: -0.1064
REMARK 3 S31: -0.1754 S32: 0.0455 S33: 0.0150
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 300:329)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8818 6.7050 -33.0506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0498 T22: 0.1338
REMARK 3 T33: 0.1491 T12: -0.0243
REMARK 3 T13: 0.0021 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.4933 L22: 4.4708
REMARK 3 L33: 6.4960 L12: 0.7626
REMARK 3 L13: -1.1052 L23: 0.3563
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0688 S13: 0.2044
REMARK 3 S21: 0.0651 S22: 0.0848 S23: -0.3424
REMARK 3 S31: 0.0167 S32: 0.3657 S33: -0.0395
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 3:80)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4041 -44.8572 -15.4581
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.0962
REMARK 3 T33: 0.1347 T12: -0.0086
REMARK 3 T13: -0.0220 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 2.2728 L22: 1.6320
REMARK 3 L33: 3.1029 L12: 0.2796
REMARK 3 L13: -1.3314 L23: -0.1003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0432 S12: -0.1383 S13: -0.0222
REMARK 3 S21: 0.0892 S22: 0.0106 S23: -0.2462
REMARK 3 S31: 0.0442 S32: 0.2054 S33: 0.0296
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 81:131)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4628 -42.2244 -7.0521
REMARK 3 T TENSOR
REMARK 3 T11: 0.1269 T22: 0.1506
REMARK 3 T33: 0.1243 T12: -0.0124
REMARK 3 T13: 0.0441 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 3.3344 L22: 3.7267
REMARK 3 L33: 4.4054 L12: -0.6212
REMARK 3 L13: 1.2095 L23: 1.0278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.2232 S13: 0.4041
REMARK 3 S21: 0.1322 S22: 0.0570 S23: 0.2260
REMARK 3 S31: -0.2644 S32: -0.2131 S33: -0.0353
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 132:299)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8285 -29.8726 -30.0776
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.1532
REMARK 3 T33: 0.1443 T12: -0.0154
REMARK 3 T13: 0.0062 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.1154 L22: 2.5207
REMARK 3 L33: 1.6362 L12: 1.0741
REMARK 3 L13: 0.3894 L23: -0.5028
REMARK 3 S TENSOR
REMARK 3 S11: -0.1608 S12: 0.3473 S13: 0.0345
REMARK 3 S21: -0.2737 S22: 0.1420 S23: 0.1054
REMARK 3 S31: -0.1706 S32: 0.0407 S33: 0.0094
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 300:329)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0259 -51.1172 -25.0133
REMARK 3 T TENSOR
REMARK 3 T11: 0.1722 T22: 0.1270
REMARK 3 T33: 0.1223 T12: 0.0094
REMARK 3 T13: -0.0488 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 5.4470 L22: 3.7383
REMARK 3 L33: 1.9377 L12: -0.2017
REMARK 3 L13: -0.3156 L23: -0.2008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.4281 S13: -0.2269
REMARK 3 S21: -0.1914 S22: -0.0958 S23: 0.0767
REMARK 3 S31: 0.2383 S32: -0.1159 S33: -0.0295
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 4:97 OR RESSEQ
REMARK 3 104:150 OR RESSEQ 157:328)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 4:97 OR RESSEQ
REMARK 3 104:150 OR RESSEQ 157:328)
REMARK 3 ATOM PAIRS NUMBER : 2247
REMARK 3 RMSD : 0.085
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5A3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1290063960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : DOUBLE SI 1 1 1
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28266
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 42.267
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 6.640
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.690
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M TRIS-HCL
REMARK 280 PH 8.5, 32% PEG4000 (V/V)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.36000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.32500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.36000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.32500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 104.94500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.36000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.32500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.94500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.36000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.32500
REMARK 290 SMTRY3 8 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: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.2 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 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 4 CG CD CE NZ
REMARK 470 LYS A 156 CG CD CE NZ
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 OG1 THR B 322 O HOH B 2170 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN A 10 OE2 GLU A 22 3554 2.14
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 ALA A 70 142.93 87.85
REMARK 500 PRO A 132 -71.89 -55.03
REMARK 500 ASN A 144 -80.20 -97.02
REMARK 500 ASP A 151 -140.43 -84.92
REMARK 500 THR A 153 -102.54 -70.89
REMARK 500 ALA B 70 140.63 86.15
REMARK 500 HIS B 99 17.69 49.28
REMARK 500 ASN B 144 -79.85 -97.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2187 DISTANCE = 6.24 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A3J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CHLOROPLASTIC GAMMA-KETOL REDUCTASE FROM
REMARK 900 ARABIDOPSIS THALIANA BOUND TO 13-OXO-9 (Z),11(E),15(Z)-
REMARK 900 OCTADECATRIENOIC ACID.
REMARK 900 RELATED ID: 5A4D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CHLOROPLASTIC GAMMA-KETOL REDUCTASE FROM
REMARK 900 ARABIDOPSIS THALIANA BOUND TO 13KOTE AND NADP
DBREF 5A3V A 1 329 UNP Q9SV68 QORH_ARATH 1 329
DBREF 5A3V B 1 329 UNP Q9SV68 QORH_ARATH 1 329
SEQRES 1 A 329 MET ALA GLY LYS LEU MET HIS ALA LEU GLN TYR ASN SER
SEQRES 2 A 329 TYR GLY GLY GLY ALA ALA GLY LEU GLU HIS VAL GLN VAL
SEQRES 3 A 329 PRO VAL PRO THR PRO LYS SER ASN GLU VAL CYS LEU LYS
SEQRES 4 A 329 LEU GLU ALA THR SER LEU ASN PRO VAL ASP TRP LYS ILE
SEQRES 5 A 329 GLN LYS GLY MET ILE ARG PRO PHE LEU PRO ARG LYS PHE
SEQRES 6 A 329 PRO CYS ILE PRO ALA THR ASP VAL ALA GLY GLU VAL VAL
SEQRES 7 A 329 GLU VAL GLY SER GLY VAL LYS ASN PHE LYS ALA GLY ASP
SEQRES 8 A 329 LYS VAL VAL ALA VAL LEU SER HIS LEU GLY GLY GLY GLY
SEQRES 9 A 329 LEU ALA GLU PHE ALA VAL ALA THR GLU LYS LEU THR VAL
SEQRES 10 A 329 LYS ARG PRO GLN GLU VAL GLY ALA ALA GLU ALA ALA ALA
SEQRES 11 A 329 LEU PRO VAL ALA GLY LEU THR ALA LEU GLN ALA LEU THR
SEQRES 12 A 329 ASN PRO ALA GLY LEU LYS LEU ASP GLY THR GLY LYS LYS
SEQRES 13 A 329 ALA ASN ILE LEU VAL THR ALA ALA SER GLY GLY VAL GLY
SEQRES 14 A 329 HIS TYR ALA VAL GLN LEU ALA LYS LEU ALA ASN ALA HIS
SEQRES 15 A 329 VAL THR ALA THR CYS GLY ALA ARG ASN ILE GLU PHE VAL
SEQRES 16 A 329 LYS SER LEU GLY ALA ASP GLU VAL LEU ASP TYR LYS THR
SEQRES 17 A 329 PRO GLU GLY ALA ALA LEU LYS SER PRO SER GLY LYS LYS
SEQRES 18 A 329 TYR ASP ALA VAL VAL HIS CYS ALA ASN GLY ILE PRO PHE
SEQRES 19 A 329 SER VAL PHE GLU PRO ASN LEU SER GLU ASN GLY LYS VAL
SEQRES 20 A 329 ILE ASP ILE THR PRO GLY PRO ASN ALA MET TRP THR TYR
SEQRES 21 A 329 ALA VAL LYS LYS ILE THR MET SER LYS LYS GLN LEU VAL
SEQRES 22 A 329 PRO LEU LEU LEU ILE PRO LYS ALA GLU ASN LEU GLU PHE
SEQRES 23 A 329 MET VAL ASN LEU VAL LYS GLU GLY LYS VAL LYS THR VAL
SEQRES 24 A 329 ILE ASP SER LYS HIS PRO LEU SER LYS ALA GLU ASP ALA
SEQRES 25 A 329 TRP ALA LYS SER ILE ASP GLY HIS ALA THR GLY LYS ILE
SEQRES 26 A 329 ILE VAL GLU PRO
SEQRES 1 B 329 MET ALA GLY LYS LEU MET HIS ALA LEU GLN TYR ASN SER
SEQRES 2 B 329 TYR GLY GLY GLY ALA ALA GLY LEU GLU HIS VAL GLN VAL
SEQRES 3 B 329 PRO VAL PRO THR PRO LYS SER ASN GLU VAL CYS LEU LYS
SEQRES 4 B 329 LEU GLU ALA THR SER LEU ASN PRO VAL ASP TRP LYS ILE
SEQRES 5 B 329 GLN LYS GLY MET ILE ARG PRO PHE LEU PRO ARG LYS PHE
SEQRES 6 B 329 PRO CYS ILE PRO ALA THR ASP VAL ALA GLY GLU VAL VAL
SEQRES 7 B 329 GLU VAL GLY SER GLY VAL LYS ASN PHE LYS ALA GLY ASP
SEQRES 8 B 329 LYS VAL VAL ALA VAL LEU SER HIS LEU GLY GLY GLY GLY
SEQRES 9 B 329 LEU ALA GLU PHE ALA VAL ALA THR GLU LYS LEU THR VAL
SEQRES 10 B 329 LYS ARG PRO GLN GLU VAL GLY ALA ALA GLU ALA ALA ALA
SEQRES 11 B 329 LEU PRO VAL ALA GLY LEU THR ALA LEU GLN ALA LEU THR
SEQRES 12 B 329 ASN PRO ALA GLY LEU LYS LEU ASP GLY THR GLY LYS LYS
SEQRES 13 B 329 ALA ASN ILE LEU VAL THR ALA ALA SER GLY GLY VAL GLY
SEQRES 14 B 329 HIS TYR ALA VAL GLN LEU ALA LYS LEU ALA ASN ALA HIS
SEQRES 15 B 329 VAL THR ALA THR CYS GLY ALA ARG ASN ILE GLU PHE VAL
SEQRES 16 B 329 LYS SER LEU GLY ALA ASP GLU VAL LEU ASP TYR LYS THR
SEQRES 17 B 329 PRO GLU GLY ALA ALA LEU LYS SER PRO SER GLY LYS LYS
SEQRES 18 B 329 TYR ASP ALA VAL VAL HIS CYS ALA ASN GLY ILE PRO PHE
SEQRES 19 B 329 SER VAL PHE GLU PRO ASN LEU SER GLU ASN GLY LYS VAL
SEQRES 20 B 329 ILE ASP ILE THR PRO GLY PRO ASN ALA MET TRP THR TYR
SEQRES 21 B 329 ALA VAL LYS LYS ILE THR MET SER LYS LYS GLN LEU VAL
SEQRES 22 B 329 PRO LEU LEU LEU ILE PRO LYS ALA GLU ASN LEU GLU PHE
SEQRES 23 B 329 MET VAL ASN LEU VAL LYS GLU GLY LYS VAL LYS THR VAL
SEQRES 24 B 329 ILE ASP SER LYS HIS PRO LEU SER LYS ALA GLU ASP ALA
SEQRES 25 B 329 TRP ALA LYS SER ILE ASP GLY HIS ALA THR GLY LYS ILE
SEQRES 26 B 329 ILE VAL GLU PRO
FORMUL 3 HOH *387(H2 O)
HELIX 1 1 GLY A 17 LEU A 21 5 5
HELIX 2 2 ASN A 46 GLY A 55 1 10
HELIX 3 3 SER A 98 GLY A 101 5 4
HELIX 4 4 GLY A 124 ALA A 130 1 7
HELIX 5 5 LEU A 131 ASN A 144 1 14
HELIX 6 6 GLY A 166 ALA A 179 1 14
HELIX 7 7 GLY A 188 ARG A 190 5 3
HELIX 8 8 ASN A 191 LEU A 198 1 8
HELIX 9 9 THR A 208 LEU A 214 1 7
HELIX 10 10 PRO A 233 GLU A 238 1 6
HELIX 11 11 GLY A 253 MET A 267 1 15
HELIX 12 12 LYS A 280 GLU A 293 1 14
HELIX 13 13 LYS A 308 GLY A 319 1 12
HELIX 14 14 GLY B 17 LEU B 21 5 5
HELIX 15 15 ASN B 46 GLY B 55 1 10
HELIX 16 16 SER B 98 GLY B 101 5 4
HELIX 17 17 GLY B 124 ALA B 130 1 7
HELIX 18 18 LEU B 131 ASN B 144 1 14
HELIX 19 19 GLY B 166 ALA B 179 1 14
HELIX 20 20 GLY B 188 ARG B 190 5 3
HELIX 21 21 ASN B 191 LEU B 198 1 8
HELIX 22 22 THR B 208 LEU B 214 1 7
HELIX 23 23 PRO B 233 GLU B 238 1 6
HELIX 24 24 GLY B 253 MET B 267 1 15
HELIX 25 25 LYS B 280 GLU B 293 1 14
HELIX 26 26 LYS B 308 GLY B 319 1 12
SHEET 1 AA 2 LEU A 5 GLN A 10 0
SHEET 2 AA 2 GLU A 22 PRO A 27 -1 O GLU A 22 N GLN A 10
SHEET 1 AB 2 PHE A 108 THR A 112 0
SHEET 2 AB 2 GLU A 35 SER A 44 -1 O VAL A 36 N ALA A 111
SHEET 1 AC 6 THR A 116 LYS A 118 0
SHEET 2 AC 6 LYS A 92 VAL A 96 -1 O VAL A 94 N VAL A 117
SHEET 3 AC 6 ASP A 72 VAL A 80 -1 O VAL A 73 N ALA A 95
SHEET 4 AC 6 GLU A 35 SER A 44 -1 O CYS A 37 N VAL A 78
SHEET 5 AC 6 LYS A 324 GLU A 328 -1 O VAL A 327 N THR A 43
SHEET 6 AC 6 ILE A 300 PRO A 305 1 N ASP A 301 O LYS A 324
SHEET 1 AD 5 THR A 116 LYS A 118 0
SHEET 2 AD 5 LYS A 92 VAL A 96 -1 O VAL A 94 N VAL A 117
SHEET 3 AD 5 ASP A 72 VAL A 80 -1 O VAL A 73 N ALA A 95
SHEET 4 AD 5 GLU A 35 SER A 44 -1 O CYS A 37 N VAL A 78
SHEET 5 AD 5 PHE A 108 THR A 112 -1 O ALA A 109 N LEU A 38
SHEET 1 AE 6 GLU A 202 ASP A 205 0
SHEET 2 AE 6 HIS A 182 CYS A 187 1 O VAL A 183 N GLU A 202
SHEET 3 AE 6 ASN A 158 THR A 162 1 O ILE A 159 N THR A 184
SHEET 4 AE 6 TYR A 222 HIS A 227 1 N ASP A 223 O ASN A 158
SHEET 5 AE 6 LEU A 241 ILE A 250 1 N SER A 242 O TYR A 222
SHEET 6 AE 6 GLN A 271 LEU A 275 1 O GLN A 271 N VAL A 247
SHEET 1 BA 2 LEU B 5 GLN B 10 0
SHEET 2 BA 2 GLU B 22 PRO B 27 -1 O GLU B 22 N GLN B 10
SHEET 1 BB 2 PHE B 108 THR B 112 0
SHEET 2 BB 2 GLU B 35 SER B 44 -1 O VAL B 36 N ALA B 111
SHEET 1 BC 6 THR B 116 LYS B 118 0
SHEET 2 BC 6 LYS B 92 VAL B 96 -1 O VAL B 94 N VAL B 117
SHEET 3 BC 6 ASP B 72 VAL B 80 -1 O VAL B 73 N ALA B 95
SHEET 4 BC 6 GLU B 35 SER B 44 -1 O CYS B 37 N VAL B 78
SHEET 5 BC 6 LYS B 324 GLU B 328 -1 O VAL B 327 N THR B 43
SHEET 6 BC 6 ILE B 300 PRO B 305 1 N ASP B 301 O LYS B 324
SHEET 1 BD 5 THR B 116 LYS B 118 0
SHEET 2 BD 5 LYS B 92 VAL B 96 -1 O VAL B 94 N VAL B 117
SHEET 3 BD 5 ASP B 72 VAL B 80 -1 O VAL B 73 N ALA B 95
SHEET 4 BD 5 GLU B 35 SER B 44 -1 O CYS B 37 N VAL B 78
SHEET 5 BD 5 PHE B 108 THR B 112 -1 O ALA B 109 N LEU B 38
SHEET 1 BE 6 GLU B 202 ASP B 205 0
SHEET 2 BE 6 HIS B 182 CYS B 187 1 O VAL B 183 N GLU B 202
SHEET 3 BE 6 ASN B 158 THR B 162 1 O ILE B 159 N THR B 184
SHEET 4 BE 6 TYR B 222 HIS B 227 1 N ASP B 223 O ASN B 158
SHEET 5 BE 6 LEU B 241 ILE B 250 1 N SER B 242 O TYR B 222
SHEET 6 BE 6 GLN B 271 LEU B 275 1 O GLN B 271 N VAL B 247
CISPEP 1 ARG A 58 PRO A 59 0 -1.60
CISPEP 2 ARG A 58 PRO A 59 0 -6.60
CISPEP 3 LEU A 61 PRO A 62 0 -7.11
CISPEP 4 PHE A 65 PRO A 66 0 -0.92
CISPEP 5 GLU A 328 PRO A 329 0 -4.45
CISPEP 6 ARG B 58 PRO B 59 0 2.18
CISPEP 7 LEU B 61 PRO B 62 0 -5.36
CISPEP 8 PHE B 65 PRO B 66 0 1.62
CISPEP 9 GLU B 328 PRO B 329 0 -7.96
CRYST1 44.720 142.650 209.890 90.00 90.00 90.00 C 2 2 21 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 0.022361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004764 0.00000
MTRIX1 1 0.125100 -0.507900 -0.852300 -41.39000 1
MTRIX2 1 -0.499800 -0.774400 0.388000 -31.20000 1
MTRIX3 1 -0.857100 0.377400 -0.350700 -36.24000 1
(ATOM LINES ARE NOT SHOWN.)
END
