| 3EBL-pdb | HEADER HYDROLASE RECEPTOR 28-AUG-08 3EBL
TITLE CRYSTAL STRUCTURE OF RICE GID1 COMPLEXED WITH GA4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GIBBERELLIN RECEPTOR GID1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: GIBBERELLIN-INSENSITIVE DWARF PROTEIN 1, PROTEIN
COMPND 5 GIBBERELLIN INSENSITIVE DWARF1;
COMPND 6 EC: 3.-.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 GENE: GID1, OS05G0407500, LOC_OS05G33730, OJ1657_H11.10,
SOURCE 5 P0040B10.6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS ALPHA/BETA HYDROLASE, LIPASE, GIBBERELLIN SIGNALING PATHWAY,
KEYWDS 2 HYDROLASE, NUCLEUS, RECEPTOR, HYDROLASE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHIMADA,T.NAKATSU,M.UEGUCHI-TANAKA,H.KATO,M.MATSUOKA
REVDAT 1 25-NOV-08 3EBL 0
JRNL AUTH A.SHIMADA,M.UEGUCHI-TANAKA,T.NAKATSU,M.NAKAJIMA,
JRNL AUTH 2 Y.NAOE,H.OHMIYA,H.KATO,M.MATSUOKA
JRNL TITL STRUCTURAL BASIS FOR GIBBERELLIN RECOGNITION BY
JRNL TITL 2 ITS RECEPTOR GID1
JRNL REF NATURE
JRNL REFN ASTM NATUAS UK ESSN 1476-4687
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 183960
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9761
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 662
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 16004
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.36000
REMARK 3 B33 (A**2) : -1.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.718
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15244 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20780 ; 1.507 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1861 ; 6.006 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 719 ;31.682 ;22.656
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2222 ;14.117 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 126 ;16.973 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2262 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11855 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7195 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10336 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1241 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.129 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.082 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9551 ; 0.928 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14912 ; 1.569 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6437 ; 2.211 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5868 ; 3.188 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EBL COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB049119.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-2008
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ASDC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 193933
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 8% MPD, 0.2M NANO3,
REMARK 280 0.1M HEPES PH7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
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,1/2+Y,-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 66.94750
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, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 ASP A 5
REMARK 465 GLU A 6
REMARK 465 VAL A 7
REMARK 465 ASN A 8
REMARK 465 ARG A 9
REMARK 465 ASN A 10
REMARK 465 GLU A 11
REMARK 465 CYS A 12
REMARK 465 LYS A 13
REMARK 465 THR A 14
REMARK 465 ALA A 85
REMARK 465 GLU A 86
REMARK 465 GLY A 87
REMARK 465 ASP A 88
REMARK 465 ALA A 89
REMARK 465 GLU A 90
REMARK 465 GLU A 91
REMARK 465 GLY A 92
REMARK 465 ALA A 93
REMARK 465 ALA A 94
REMARK 465 ALA A 95
REMARK 465 VAL A 96
REMARK 465 THR A 97
REMARK 465 ARG A 98
REMARK 465 PRO A 99
REMARK 465 ILE A 100
REMARK 465 TYR A 354
REMARK 465 GLY A 355
REMARK 465 SER A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 ASP B 5
REMARK 465 GLU B 6
REMARK 465 VAL B 7
REMARK 465 ASN B 8
REMARK 465 ARG B 9
REMARK 465 ASN B 10
REMARK 465 GLU B 11
REMARK 465 CYS B 12
REMARK 465 LYS B 13
REMARK 465 ALA B 85
REMARK 465 GLU B 86
REMARK 465 GLY B 87
REMARK 465 ASP B 88
REMARK 465 ALA B 89
REMARK 465 GLU B 90
REMARK 465 GLU B 91
REMARK 465 GLY B 92
REMARK 465 ALA B 93
REMARK 465 ALA B 94
REMARK 465 ALA B 95
REMARK 465 VAL B 96
REMARK 465 THR B 97
REMARK 465 ARG B 98
REMARK 465 PRO B 99
REMARK 465 ILE B 100
REMARK 465 LEU B 101
REMARK 465 GLU B 102
REMARK 465 GLY B 185
REMARK 465 GLY B 186
REMARK 465 ASP B 187
REMARK 465 TYR B 353
REMARK 465 TYR B 354
REMARK 465 GLY B 355
REMARK 465 SER B 356
REMARK 465 HIS B 357
REMARK 465 HIS B 358
REMARK 465 HIS B 359
REMARK 465 HIS B 360
REMARK 465 HIS B 361
REMARK 465 HIS B 362
REMARK 465 HIS B 363
REMARK 465 HIS B 364
REMARK 465 HIS B 365
REMARK 465 HIS B 366
REMARK 465 ALA C 2
REMARK 465 GLY C 3
REMARK 465 SER C 4
REMARK 465 ASP C 5
REMARK 465 GLU C 6
REMARK 465 VAL C 7
REMARK 465 ASN C 8
REMARK 465 ARG C 9
REMARK 465 ASN C 10
REMARK 465 GLU C 11
REMARK 465 CYS C 12
REMARK 465 LYS C 13
REMARK 465 THR C 14
REMARK 465 VAL C 15
REMARK 465 ALA C 84
REMARK 465 ALA C 85
REMARK 465 GLU C 86
REMARK 465 GLY C 87
REMARK 465 ASP C 88
REMARK 465 ALA C 89
REMARK 465 GLU C 90
REMARK 465 GLU C 91
REMARK 465 GLY C 92
REMARK 465 ALA C 93
REMARK 465 ALA C 94
REMARK 465 ALA C 95
REMARK 465 VAL C 96
REMARK 465 THR C 97
REMARK 465 ARG C 98
REMARK 465 PRO C 99
REMARK 465 ILE C 100
REMARK 465 LEU C 101
REMARK 465 GLU C 102
REMARK 465 PHE C 103
REMARK 465 LEU C 104
REMARK 465 THR C 105
REMARK 465 ASP C 106
REMARK 465 ALA C 107
REMARK 465 PRO C 108
REMARK 465 ALA C 109
REMARK 465 ALA C 110
REMARK 465 GLU C 111
REMARK 465 PRO C 112
REMARK 465 SER C 184
REMARK 465 GLY C 185
REMARK 465 GLY C 186
REMARK 465 ASP C 187
REMARK 465 ALA C 188
REMARK 465 GLN C 189
REMARK 465 LEU C 352
REMARK 465 TYR C 353
REMARK 465 TYR C 354
REMARK 465 GLY C 355
REMARK 465 SER C 356
REMARK 465 HIS C 357
REMARK 465 HIS C 358
REMARK 465 HIS C 359
REMARK 465 HIS C 360
REMARK 465 HIS C 361
REMARK 465 HIS C 362
REMARK 465 HIS C 363
REMARK 465 HIS C 364
REMARK 465 HIS C 365
REMARK 465 HIS C 366
REMARK 465 ALA D 2
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 ASP D 5
REMARK 465 GLU D 6
REMARK 465 VAL D 7
REMARK 465 ASN D 8
REMARK 465 ARG D 9
REMARK 465 ASN D 10
REMARK 465 GLU D 11
REMARK 465 CYS D 12
REMARK 465 LYS D 13
REMARK 465 THR D 14
REMARK 465 ALA D 85
REMARK 465 GLU D 86
REMARK 465 GLY D 87
REMARK 465 ASP D 88
REMARK 465 ALA D 89
REMARK 465 GLU D 90
REMARK 465 GLU D 91
REMARK 465 GLY D 92
REMARK 465 ALA D 93
REMARK 465 ALA D 94
REMARK 465 ALA D 95
REMARK 465 VAL D 96
REMARK 465 THR D 97
REMARK 465 ARG D 98
REMARK 465 PRO D 99
REMARK 465 ILE D 100
REMARK 465 LEU D 101
REMARK 465 GLU D 102
REMARK 465 PHE D 103
REMARK 465 LEU D 104
REMARK 465 THR D 105
REMARK 465 ASP D 106
REMARK 465 ALA D 107
REMARK 465 PRO D 108
REMARK 465 TYR D 354
REMARK 465 GLY D 355
REMARK 465 SER D 356
REMARK 465 HIS D 357
REMARK 465 HIS D 358
REMARK 465 HIS D 359
REMARK 465 HIS D 360
REMARK 465 HIS D 361
REMARK 465 HIS D 362
REMARK 465 HIS D 363
REMARK 465 HIS D 364
REMARK 465 HIS D 365
REMARK 465 HIS D 366
REMARK 465 ALA E 2
REMARK 465 GLY E 3
REMARK 465 SER E 4
REMARK 465 ASP E 5
REMARK 465 GLU E 6
REMARK 465 VAL E 7
REMARK 465 ASN E 8
REMARK 465 ARG E 9
REMARK 465 ASN E 10
REMARK 465 GLU E 11
REMARK 465 CYS E 12
REMARK 465 LYS E 13
REMARK 465 THR E 14
REMARK 465 VAL E 15
REMARK 465 ALA E 84
REMARK 465 ALA E 85
REMARK 465 GLU E 86
REMARK 465 GLY E 87
REMARK 465 ASP E 88
REMARK 465 ALA E 89
REMARK 465 GLU E 90
REMARK 465 GLU E 91
REMARK 465 GLY E 92
REMARK 465 ALA E 93
REMARK 465 ALA E 94
REMARK 465 ALA E 95
REMARK 465 VAL E 96
REMARK 465 THR E 97
REMARK 465 ARG E 98
REMARK 465 PRO E 99
REMARK 465 ILE E 100
REMARK 465 GLY E 185
REMARK 465 GLY E 186
REMARK 465 ASP E 187
REMARK 465 ALA E 188
REMARK 465 GLN E 189
REMARK 465 TYR E 353
REMARK 465 TYR E 354
REMARK 465 GLY E 355
REMARK 465 SER E 356
REMARK 465 HIS E 357
REMARK 465 HIS E 358
REMARK 465 HIS E 359
REMARK 465 HIS E 360
REMARK 465 HIS E 361
REMARK 465 HIS E 362
REMARK 465 HIS E 363
REMARK 465 HIS E 364
REMARK 465 HIS E 365
REMARK 465 HIS E 366
REMARK 465 ALA F 2
REMARK 465 GLY F 3
REMARK 465 SER F 4
REMARK 465 ASP F 5
REMARK 465 GLU F 6
REMARK 465 VAL F 7
REMARK 465 ASN F 8
REMARK 465 ARG F 9
REMARK 465 ASN F 10
REMARK 465 GLU F 11
REMARK 465 CYS F 12
REMARK 465 LYS F 13
REMARK 465 THR F 14
REMARK 465 ALA F 85
REMARK 465 GLU F 86
REMARK 465 GLY F 87
REMARK 465 ASP F 88
REMARK 465 ALA F 89
REMARK 465 GLU F 90
REMARK 465 GLU F 91
REMARK 465 GLY F 92
REMARK 465 ALA F 93
REMARK 465 ALA F 94
REMARK 465 ALA F 95
REMARK 465 VAL F 96
REMARK 465 THR F 97
REMARK 465 ARG F 98
REMARK 465 PRO F 99
REMARK 465 ILE F 100
REMARK 465 LEU F 101
REMARK 465 GLU F 102
REMARK 465 PHE F 103
REMARK 465 LEU F 104
REMARK 465 THR F 105
REMARK 465 ASP F 106
REMARK 465 ALA F 107
REMARK 465 PRO F 108
REMARK 465 ALA F 109
REMARK 465 ALA F 110
REMARK 465 GLU F 111
REMARK 465 PRO F 112
REMARK 465 SER F 184
REMARK 465 GLY F 185
REMARK 465 GLY F 186
REMARK 465 ASP F 187
REMARK 465 ALA F 188
REMARK 465 GLN F 189
REMARK 465 TYR F 354
REMARK 465 GLY F 355
REMARK 465 SER F 356
REMARK 465 HIS F 357
REMARK 465 HIS F 358
REMARK 465 HIS F 359
REMARK 465 HIS F 360
REMARK 465 HIS F 361
REMARK 465 HIS F 362
REMARK 465 HIS F 363
REMARK 465 HIS F 364
REMARK 465 HIS F 365
REMARK 465 HIS F 366
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 ARG A 58 CD NE CZ NH1 NH2
REMARK 470 LEU A 101 CG CD1 CD2
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 LEU A 104 CG CD1 CD2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 LYS A 146 CD CE NZ
REMARK 470 GLN A 189 CG CD OE1 NE2
REMARK 470 LYS A 217 CD CE NZ
REMARK 470 LYS A 243 CE NZ
REMARK 470 TYR A 353 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR B 14 OG1 CG2
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 82 CD NE CZ NH1 NH2
REMARK 470 PHE B 103 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 104 CG CD1 CD2
REMARK 470 THR B 105 OG1 CG2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 LYS B 146 CE NZ
REMARK 470 LYS B 174 CE NZ
REMARK 470 PHE B 181 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 189 CG CD OE1 NE2
REMARK 470 LYS B 217 CD CE NZ
REMARK 470 GLN B 249 CD OE1 NE2
REMARK 470 ARG C 58 NE CZ NH1 NH2
REMARK 470 ARG C 82 CD NE CZ NH1 NH2
REMARK 470 ARG C 140 CZ NH1 NH2
REMARK 470 LYS C 146 CE NZ
REMARK 470 LYS C 174 CD CE NZ
REMARK 470 PHE C 181 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 183 CD NE CZ NH1 NH2
REMARK 470 ARG C 191 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 217 CD CE NZ
REMARK 470 GLU C 232 CG CD OE1 OE2
REMARK 470 ARG C 238 CZ NH1 NH2
REMARK 470 GLU C 261 CG CD OE1 OE2
REMARK 470 VAL D 15 CG1 CG2
REMARK 470 ARG D 58 CD NE CZ NH1 NH2
REMARK 470 GLN D 72 CD OE1 NE2
REMARK 470 SER D 73 OG
REMARK 470 ARG D 82 CD NE CZ NH1 NH2
REMARK 470 GLU D 111 CD OE1 OE2
REMARK 470 LYS D 146 CE NZ
REMARK 470 LYS D 174 CE NZ
REMARK 470 LYS D 217 CD CE NZ
REMARK 470 GLU D 232 CG CD OE1 OE2
REMARK 470 ARG D 238 CD NE CZ NH1 NH2
REMARK 470 LYS D 243 CD CE NZ
REMARK 470 LYS D 256 CE NZ
REMARK 470 LYS D 287 CE NZ
REMARK 470 ARG D 310 CZ NH1 NH2
REMARK 470 ARG E 58 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 72 CD OE1 NE2
REMARK 470 SER E 73 OG
REMARK 470 ARG E 82 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 101 CG CD1 CD2
REMARK 470 GLU E 102 CG CD OE1 OE2
REMARK 470 PHE E 103 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU E 104 CG CD1 CD2
REMARK 470 THR E 105 OG1 CG2
REMARK 470 ASP E 106 CG OD1 OD2
REMARK 470 GLU E 111 CG CD OE1 OE2
REMARK 470 ARG E 140 CZ NH1 NH2
REMARK 470 LYS E 143 CE NZ
REMARK 470 LYS E 174 CD CE NZ
REMARK 470 PHE E 181 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 183 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 191 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 214 CG CD OE1 OE2
REMARK 470 LYS E 217 CG CD CE NZ
REMARK 470 GLU E 232 CG CD OE1 OE2
REMARK 470 ARG E 238 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 243 CD CE NZ
REMARK 470 GLN E 249 OE1 NE2
REMARK 470 LYS E 256 CE NZ
REMARK 470 ASP E 262 CG OD1 OD2
REMARK 470 ASN E 276 CG OD1 ND2
REMARK 470 LYS E 287 CG CD CE NZ
REMARK 470 ARG E 310 CG CD NE CZ NH1 NH2
REMARK 470 HIS E 315 CG ND1 CD2 CE1 NE2
REMARK 470 LYS E 317 CD CE NZ
REMARK 470 ASN E 349 CG OD1 ND2
REMARK 470 VAL F 15 CG1 CG2
REMARK 470 ARG F 58 CD NE CZ NH1 NH2
REMARK 470 SER F 73 OG
REMARK 470 VAL F 74 CG1 CG2
REMARK 470 ARG F 82 CD NE CZ NH1 NH2
REMARK 470 ARG F 140 CZ NH1 NH2
REMARK 470 LYS F 143 CE NZ
REMARK 470 LYS F 146 CE NZ
REMARK 470 LYS F 174 CE NZ
REMARK 470 PHE F 181 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS F 217 CG CD CE NZ
REMARK 470 GLU F 232 CG CD OE1 OE2
REMARK 470 ARG F 238 CD NE CZ NH1 NH2
REMARK 470 LYS F 243 CE NZ
REMARK 470 GLN F 249 CD OE1 NE2
REMARK 470 LYS F 256 CE NZ
REMARK 470 GLU F 261 CD OE1 OE2
REMARK 470 CYS F 270 SG
REMARK 470 ARG F 279 CZ NH1 NH2
REMARK 470 ARG F 310 CZ NH1 NH2
REMARK 470 GLU F 322 CG CD OE1 OE2
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 106 150.99 -44.31
REMARK 500 PHE A 124 -6.60 74.38
REMARK 500 SER A 127 179.72 69.67
REMARK 500 ALA A 188 68.78 26.70
REMARK 500 SER A 198 -135.37 54.50
REMARK 500 PHE A 245 -28.51 79.28
REMARK 500 VAL B 15 -68.05 66.99
REMARK 500 GLU B 61 43.34 35.09
REMARK 500 ASP B 71 104.07 -163.79
REMARK 500 PRO B 108 131.19 -34.81
REMARK 500 PHE B 124 -11.25 78.79
REMARK 500 SER B 127 178.05 73.75
REMARK 500 SER B 198 -136.26 59.43
REMARK 500 PHE B 245 -26.92 80.30
REMARK 500 GLU C 61 56.34 31.16
REMARK 500 PHE C 124 -7.91 74.23
REMARK 500 SER C 127 173.25 74.21
REMARK 500 SER C 198 -132.58 54.85
REMARK 500 PHE C 245 -28.31 81.35
REMARK 500 ALA C 286 152.35 -38.59
REMARK 500 ASN C 333 15.98 -140.99
REMARK 500 PHE D 124 -12.40 83.18
REMARK 500 SER D 127 176.60 78.09
REMARK 500 SER D 198 -131.13 53.22
REMARK 500 PHE D 245 -27.24 76.82
REMARK 500 GLU E 61 45.25 39.77
REMARK 500 PRO E 108 155.52 -49.59
REMARK 500 PHE E 124 -11.23 81.32
REMARK 500 SER E 127 176.59 77.35
REMARK 500 LYS E 146 29.61 48.85
REMARK 500 SER E 198 -138.57 53.88
REMARK 500 PHE E 245 -32.87 76.92
REMARK 500 ASP E 264 -168.73 -126.03
REMARK 500 PHE F 124 -12.58 75.37
REMARK 500 SER F 127 172.61 73.96
REMARK 500 SER F 198 -133.17 55.88
REMARK 500 PHE F 245 -28.32 80.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 601
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 602
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 603
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 604
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 B 401
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 501
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 601
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 602
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 604
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 701
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 C 401
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 501
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 601
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 602
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 603
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 604
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 D 401
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 501
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 601
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 602
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 603
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 701
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 E 401
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 501
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 601
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 F 401
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 501
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 601
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 602
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 603
DBREF 3EBL A 2 354 UNP Q6L545 GID1_ORYSJ 2 354
DBREF 3EBL B 2 354 UNP Q6L545 GID1_ORYSJ 2 354
DBREF 3EBL C 2 354 UNP Q6L545 GID1_ORYSJ 2 354
DBREF 3EBL D 2 354 UNP Q6L545 GID1_ORYSJ 2 354
DBREF 3EBL E 2 354 UNP Q6L545 GID1_ORYSJ 2 354
DBREF 3EBL F 2 354 UNP Q6L545 GID1_ORYSJ 2 354
SEQADV 3EBL GLY A 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER A 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS A 366 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL GLY B 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER B 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS B 366 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL GLY C 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER C 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS C 366 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL GLY D 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER D 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS D 366 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL GLY E 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER E 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS E 366 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL GLY F 355 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL SER F 356 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 357 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 358 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 359 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 360 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 361 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 362 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 363 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 364 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 365 UNP Q6L545 EXPRESSION TAG
SEQADV 3EBL HIS F 366 UNP Q6L545 EXPRESSION TAG
SEQRES 1 A 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 A 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 A 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 A 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 A 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 A 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 A 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 A 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 A 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 A 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 A 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 A 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 A 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 A 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 A 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 A 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 A 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 A 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 A 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 A 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 A 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 A 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 A 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 A 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 A 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 A 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 A 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 A 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 A 365 HIS
SEQRES 1 B 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 B 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 B 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 B 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 B 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 B 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 B 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 B 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 B 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 B 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 B 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 B 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 B 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 B 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 B 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 B 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 B 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 B 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 B 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 B 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 B 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 B 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 B 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 B 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 B 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 B 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 B 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 B 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 B 365 HIS
SEQRES 1 C 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 C 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 C 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 C 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 C 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 C 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 C 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 C 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 C 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 C 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 C 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 C 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 C 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 C 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 C 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 C 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 C 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 C 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 C 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 C 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 C 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 C 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 C 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 C 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 C 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 C 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 C 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 C 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 C 365 HIS
SEQRES 1 D 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 D 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 D 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 D 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 D 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 D 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 D 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 D 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 D 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 D 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 D 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 D 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 D 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 D 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 D 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 D 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 D 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 D 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 D 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 D 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 D 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 D 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 D 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 D 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 D 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 D 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 D 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 D 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 D 365 HIS
SEQRES 1 E 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 E 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 E 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 E 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 E 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 E 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 E 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 E 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 E 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 E 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 E 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 E 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 E 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 E 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 E 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 E 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 E 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 E 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 E 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 E 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 E 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 E 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 E 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 E 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 E 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 E 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 E 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 E 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 E 365 HIS
SEQRES 1 F 365 ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR
SEQRES 2 F 365 VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE
SEQRES 3 F 365 LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR
SEQRES 4 F 365 PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL
SEQRES 5 F 365 PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE
SEQRES 6 F 365 ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG
SEQRES 7 F 365 ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY
SEQRES 8 F 365 ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR
SEQRES 9 F 365 ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE
SEQRES 10 F 365 PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER
SEQRES 11 F 365 THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU
SEQRES 12 F 365 SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA
SEQRES 13 F 365 PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP
SEQRES 14 F 365 THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG
SEQRES 15 F 365 SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY
SEQRES 16 F 365 ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL
SEQRES 17 F 365 ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE
SEQRES 18 F 365 LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU
SEQRES 19 F 365 SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU
SEQRES 20 F 365 GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU
SEQRES 21 F 365 ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY
SEQRES 22 F 365 PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS
SEQRES 23 F 365 SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP
SEQRES 24 F 365 ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY
SEQRES 25 F 365 HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL
SEQRES 26 F 365 GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU
SEQRES 27 F 365 VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU
SEQRES 28 F 365 TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 29 F 365 HIS
HET GA4 A 401 24
HET MPD A 501 8
HET NO3 A 601 4
HET NO3 A 602 4
HET NO3 A 603 4
HET NO3 A 604 4
HET GA4 B 401 24
HET MPD B 501 8
HET NO3 B 601 4
HET NO3 B 602 4
HET NO3 B 604 4
HET PO4 B 701 5
HET GA4 C 401 24
HET MPD C 501 8
HET NO3 C 601 4
HET NO3 C 602 4
HET NO3 C 603 4
HET NO3 C 604 4
HET GA4 D 401 24
HET MPD D 501 8
HET NO3 D 601 4
HET NO3 D 602 4
HET NO3 D 603 4
HET PO4 E 701 5
HET GA4 E 401 24
HET MPD E 501 8
HET NO3 E 601 4
HET GA4 F 401 24
HET MPD F 501 8
HET NO3 F 601 4
HET NO3 F 602 4
HET NO3 F 603 4
HETNAM GA4 GIBBERELLIN A4
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM NO3 NITRATE ION
HETNAM PO4 PHOSPHATE ION
FORMUL 7 GA4 6(C19 H24 O5)
FORMUL 8 MPD 6(C6 H14 O2)
FORMUL 9 NO3 18(N O3 1-)
FORMUL 18 PO4 2(O4 P 3-)
FORMUL 39 HOH *1133(H2 O)
HELIX 1 1 PRO A 17 ARG A 35 1 19
HELIX 2 2 GLU A 42 ASP A 50 1 9
HELIX 3 3 LEU A 101 ASP A 106 5 6
HELIX 4 4 SER A 131 LYS A 146 1 16
HELIX 5 5 PRO A 163 GLN A 179 1 17
HELIX 6 6 SER A 199 GLU A 214 1 16
HELIX 7 7 THR A 234 ASP A 241 1 8
HELIX 8 8 THR A 247 LEU A 259 1 13
HELIX 9 9 THR A 298 ASP A 312 1 15
HELIX 10 10 GLY A 327 LEU A 331 5 5
HELIX 11 11 THR A 334 TYR A 353 1 20
HELIX 12 12 PRO B 17 ARG B 35 1 19
HELIX 13 13 GLU B 42 ASP B 50 1 9
HELIX 14 14 SER B 131 LYS B 146 1 16
HELIX 15 15 PRO B 163 SER B 178 1 16
HELIX 16 16 GLN B 179 ARG B 183 5 5
HELIX 17 17 SER B 198 GLU B 214 1 17
HELIX 18 18 THR B 234 ASP B 241 1 8
HELIX 19 19 THR B 247 LEU B 259 1 13
HELIX 20 20 THR B 298 ASP B 312 1 15
HELIX 21 21 GLY B 327 LEU B 331 5 5
HELIX 22 22 THR B 334 ASN B 351 1 18
HELIX 23 23 PRO C 17 ARG C 35 1 19
HELIX 24 24 GLU C 42 ASP C 50 1 9
HELIX 25 25 SER C 131 LYS C 146 1 16
HELIX 26 26 PRO C 163 GLN C 179 1 17
HELIX 27 27 PRO C 180 ARG C 183 5 4
HELIX 28 28 SER C 198 GLU C 214 1 17
HELIX 29 29 THR C 234 ASP C 241 1 8
HELIX 30 30 THR C 247 LEU C 259 1 13
HELIX 31 31 THR C 298 ASP C 312 1 15
HELIX 32 32 GLY C 327 LEU C 331 5 5
HELIX 33 33 THR C 334 ASN C 351 1 18
HELIX 34 34 PRO D 17 ARG D 35 1 19
HELIX 35 35 GLU D 42 ASP D 50 1 9
HELIX 36 36 SER D 131 LYS D 146 1 16
HELIX 37 37 PRO D 163 GLN D 179 1 17
HELIX 38 38 PRO D 180 ARG D 183 5 4
HELIX 39 39 SER D 199 GLU D 214 1 16
HELIX 40 40 THR D 234 ASP D 241 1 8
HELIX 41 41 THR D 247 LEU D 259 1 13
HELIX 42 42 THR D 298 ASP D 312 1 15
HELIX 43 43 GLY D 327 LEU D 331 5 5
HELIX 44 44 THR D 334 LEU D 352 1 19
HELIX 45 45 PRO E 17 ILE E 33 1 17
HELIX 46 46 GLU E 42 ASP E 50 1 9
HELIX 47 47 LEU E 101 ASP E 106 5 6
HELIX 48 48 SER E 131 LYS E 146 1 16
HELIX 49 49 PRO E 163 SER E 178 1 16
HELIX 50 50 GLN E 179 ARG E 183 5 5
HELIX 51 51 SER E 199 GLU E 214 1 16
HELIX 52 52 THR E 234 ASP E 241 1 8
HELIX 53 53 THR E 247 LEU E 259 1 13
HELIX 54 54 THR E 298 ASP E 312 1 15
HELIX 55 55 GLY E 327 LEU E 331 5 5
HELIX 56 56 THR E 334 ASN E 351 1 18
HELIX 57 57 PRO F 17 ARG F 35 1 19
HELIX 58 58 GLU F 42 ASP F 50 1 9
HELIX 59 59 SER F 131 LYS F 146 1 16
HELIX 60 60 PRO F 163 SER F 178 1 16
HELIX 61 61 GLN F 179 ARG F 183 5 5
HELIX 62 62 SER F 198 GLU F 214 1 17
HELIX 63 63 THR F 234 ASP F 241 1 8
HELIX 64 64 THR F 247 LEU F 259 1 13
HELIX 65 65 THR F 298 ASP F 312 1 15
HELIX 66 66 GLY F 327 LEU F 331 5 5
HELIX 67 67 THR F 334 ASN F 351 1 18
SHEET 1 A 6 VAL A 63 ASP A 71 0
SHEET 2 A 6 LEU A 76 ALA A 83 -1 O LEU A 76 N ILE A 70
SHEET 3 A 6 VAL A 148 VAL A 152 -1 O SER A 151 N ARG A 79
SHEET 4 A 6 PRO A 114 PHE A 119 1 N ILE A 116 O VAL A 150
SHEET 5 A 6 GLN A 189 ASP A 197 1 O PHE A 193 N ILE A 117
SHEET 6 A 6 ARG A 183 SER A 184 -1 N SER A 184 O GLN A 189
SHEET 1 B 8 VAL A 63 ASP A 71 0
SHEET 2 B 8 LEU A 76 ALA A 83 -1 O LEU A 76 N ILE A 70
SHEET 3 B 8 VAL A 148 VAL A 152 -1 O SER A 151 N ARG A 79
SHEET 4 B 8 PRO A 114 PHE A 119 1 N ILE A 116 O VAL A 150
SHEET 5 B 8 GLN A 189 ASP A 197 1 O PHE A 193 N ILE A 117
SHEET 6 B 8 GLY A 220 LEU A 224 1 O ILE A 222 N LEU A 194
SHEET 7 B 8 SER A 288 SER A 293 1 O ILE A 291 N LEU A 223
SHEET 8 B 8 VAL A 316 CYS A 321 1 O CYS A 321 N VAL A 292
SHEET 1 C 8 VAL B 63 ASP B 71 0
SHEET 2 C 8 LEU B 76 ALA B 83 -1 O ILE B 80 N PHE B 66
SHEET 3 C 8 VAL B 148 ASN B 153 -1 O SER B 151 N ARG B 79
SHEET 4 C 8 PRO B 114 PHE B 119 1 N ILE B 116 O VAL B 148
SHEET 5 C 8 ARG B 191 ASP B 197 1 O PHE B 193 N ILE B 117
SHEET 6 C 8 GLY B 220 LEU B 224 1 O ILE B 222 N LEU B 194
SHEET 7 C 8 SER B 288 SER B 293 1 O ILE B 291 N LEU B 223
SHEET 8 C 8 VAL B 316 CYS B 321 1 O CYS B 321 N VAL B 292
SHEET 1 D 8 SER C 64 ASP C 71 0
SHEET 2 D 8 LEU C 76 ARG C 82 -1 O ILE C 80 N PHE C 66
SHEET 3 D 8 VAL C 148 ASN C 153 -1 O SER C 151 N ARG C 79
SHEET 4 D 8 PRO C 114 PHE C 119 1 N ILE C 116 O VAL C 148
SHEET 5 D 8 ARG C 191 ASP C 197 1 O PHE C 193 N ILE C 117
SHEET 6 D 8 GLY C 220 LEU C 224 1 O LEU C 224 N GLY C 196
SHEET 7 D 8 LYS C 287 SER C 293 1 O ILE C 291 N LEU C 223
SHEET 8 D 8 VAL C 316 CYS C 321 1 O CYS C 321 N VAL C 292
SHEET 1 E 8 VAL D 63 ASP D 71 0
SHEET 2 E 8 LEU D 76 ALA D 83 -1 O ILE D 80 N PHE D 66
SHEET 3 E 8 VAL D 148 VAL D 152 -1 O SER D 151 N ARG D 79
SHEET 4 E 8 PRO D 114 PHE D 119 1 N ILE D 116 O VAL D 150
SHEET 5 E 8 ARG D 191 ASP D 197 1 O PHE D 193 N ILE D 117
SHEET 6 E 8 GLY D 220 LEU D 224 1 O ILE D 222 N LEU D 194
SHEET 7 E 8 SER D 288 SER D 293 1 O ILE D 291 N LEU D 223
SHEET 8 E 8 VAL D 316 CYS D 321 1 O LYS D 317 N ILE D 290
SHEET 1 F 8 SER E 64 ASP E 71 0
SHEET 2 F 8 LEU E 76 ARG E 82 -1 O ARG E 82 N SER E 64
SHEET 3 F 8 VAL E 148 ASN E 153 -1 O SER E 151 N ARG E 79
SHEET 4 F 8 PRO E 114 PHE E 119 1 N ILE E 116 O VAL E 150
SHEET 5 F 8 ARG E 191 SER E 198 1 O ARG E 191 N VAL E 115
SHEET 6 F 8 GLY E 220 ALA E 226 1 O ILE E 222 N LEU E 194
SHEET 7 F 8 SER E 288 SER E 293 1 O LEU E 289 N ASN E 221
SHEET 8 F 8 VAL E 316 CYS E 321 1 O LYS E 317 N SER E 288
SHEET 1 G 8 VAL F 63 ASP F 71 0
SHEET 2 G 8 LEU F 76 ALA F 83 -1 O ILE F 80 N PHE F 66
SHEET 3 G 8 VAL F 148 VAL F 152 -1 O SER F 151 N ARG F 79
SHEET 4 G 8 PRO F 114 PHE F 119 1 N ILE F 116 O VAL F 150
SHEET 5 G 8 ARG F 191 ASP F 197 1 O PHE F 193 N ILE F 117
SHEET 6 G 8 GLY F 220 LEU F 224 1 O ILE F 222 N LEU F 194
SHEET 7 G 8 SER F 288 SER F 293 1 O ILE F 291 N LEU F 223
SHEET 8 G 8 VAL F 316 CYS F 321 1 O CYS F 321 N VAL F 292
CISPEP 1 ALA A 157 PRO A 158 0 -5.07
CISPEP 2 TYR A 162 PRO A 163 0 1.19
CISPEP 3 ALA B 157 PRO B 158 0 -4.01
CISPEP 4 TYR B 162 PRO B 163 0 0.33
CISPEP 5 ALA C 157 PRO C 158 0 -3.88
CISPEP 6 TYR C 162 PRO C 163 0 -0.29
CISPEP 7 ALA D 157 PRO D 158 0 -0.69
CISPEP 8 TYR D 162 PRO D 163 0 0.88
CISPEP 9 ALA E 157 PRO E 158 0 -4.04
CISPEP 10 TYR E 162 PRO E 163 0 3.80
CISPEP 11 ALA F 157 PRO F 158 0 -8.10
CISPEP 12 TYR F 162 PRO F 163 0 3.82
SITE 1 AC1 16 ILE A 24 PHE A 27 GLY A 122 SER A 123
SITE 2 AC1 16 ILE A 133 TYR A 134 ASP A 197 SER A 198
SITE 3 AC1 16 VAL A 246 ARG A 251 TYR A 254 VAL A 326
SITE 4 AC1 16 GLY A 327 TYR A 329 HOH A 605 HOH A 607
SITE 1 AC2 6 LEU A 23 LEU A 49 ASP A 50 ARG A 51
SITE 2 AC2 6 HOH A 640 MPD B 501
SITE 1 AC3 3 ARG A 35 HOH A 785 HOH A 848
SITE 1 AC4 4 THR A 231 ASP A 264 ARG A 265 HOH A 698
SITE 1 AC5 3 ARG A 51 LEU A 331 NO3 A 604
SITE 1 AC6 6 HIS A 19 LEU A 23 ARG A 51 NO3 A 603
SITE 2 AC6 6 ASN B 26 SER B 30
SITE 1 AC7 14 ILE B 24 PHE B 27 GLY B 122 SER B 123
SITE 2 AC7 14 ILE B 133 TYR B 134 ASP B 197 SER B 198
SITE 3 AC7 14 ARG B 251 TYR B 254 VAL B 326 GLY B 327
SITE 4 AC7 14 TYR B 329 HOH B 702
SITE 1 AC8 6 MPD A 501 LEU B 23 SER B 30 LEU B 49
SITE 2 AC8 6 ARG B 51 HOH B 719
SITE 1 AC9 3 ARG B 35 TRP B 253 HOH B 891
SITE 1 BC1 4 THR B 231 ASP B 264 ARG B 265 HOH B 789
SITE 1 BC2 6 ASN A 26 SER A 30 HIS B 19 LEU B 23
SITE 2 BC2 6 ARG B 51 PO4 B 701
SITE 1 BC3 5 ARG B 51 LEU B 330 LEU B 331 NO3 B 604
SITE 2 BC3 5 HOH B 724
SITE 1 BC4 16 PHE C 27 ARG C 35 GLY C 122 SER C 123
SITE 2 BC4 16 ILE C 133 TYR C 134 ASP C 197 SER C 198
SITE 3 BC4 16 VAL C 246 ARG C 251 TYR C 254 VAL C 326
SITE 4 BC4 16 GLY C 327 TYR C 329 HOH C 605 HOH C 607
SITE 1 BC5 8 ASN C 26 SER C 30 LEU C 49 ASP C 50
SITE 2 BC5 8 ARG C 51 HOH C 638 ASN D 26 ARG D 51
SITE 1 BC6 2 ARG C 35 TRP C 253
SITE 1 BC7 4 THR C 231 ASP C 264 ARG C 265 HOH C 697
SITE 1 BC8 3 ARG C 51 LEU C 330 HOH C 642
SITE 1 BC9 5 ASN C 26 SER C 30 HIS D 19 LEU D 23
SITE 2 BC9 5 ARG D 51
SITE 1 CC1 16 ILE D 24 PHE D 27 ARG D 35 GLY D 122
SITE 2 CC1 16 SER D 123 ILE D 133 TYR D 134 ASP D 197
SITE 3 CC1 16 SER D 198 ARG D 251 TYR D 254 VAL D 326
SITE 4 CC1 16 GLY D 327 TYR D 329 HOH D 604 HOH D 606
SITE 1 CC2 6 LEU D 23 ASN D 26 LEU D 49 ASP D 50
SITE 2 CC2 6 ARG D 51 HOH D 630
SITE 1 CC3 4 ARG D 35 GLN D 249 TRP D 253 HOH D 704
SITE 1 CC4 4 THR D 231 ASP D 264 ARG D 265 HOH D 721
SITE 1 CC5 2 ARG D 51 LEU D 331
SITE 1 CC6 3 ARG E 51 SER E 136 LEU E 330
SITE 1 CC7 15 PHE E 27 ARG E 35 GLY E 122 SER E 123
SITE 2 CC7 15 ILE E 133 TYR E 134 ASP E 197 SER E 198
SITE 3 CC7 15 ARG E 251 TYR E 254 VAL E 326 GLY E 327
SITE 4 CC7 15 TYR E 329 HOH E 702 HOH E 730
SITE 1 CC8 6 ASN E 26 SER E 30 LEU E 49 ARG E 51
SITE 2 CC8 6 HOH E 711 MPD F 501
SITE 1 CC9 4 ARG E 35 GLN E 249 TRP E 253 HOH E 796
SITE 1 DC1 15 PHE F 27 GLY F 122 SER F 123 ILE F 133
SITE 2 DC1 15 TYR F 134 ASP F 197 SER F 198 PHE F 245
SITE 3 DC1 15 ARG F 251 TYR F 254 VAL F 326 GLY F 327
SITE 4 DC1 15 TYR F 329 HOH F 604 HOH F 625
SITE 1 DC2 6 MPD E 501 LEU F 23 SER F 30 LEU F 49
SITE 2 DC2 6 ARG F 51 HOH F 626
SITE 1 DC3 2 ARG F 35 HOH F 752
SITE 1 DC4 3 THR F 231 ASP F 264 ARG F 265
SITE 1 DC5 3 LEU F 330 LEU F 331 HOH F 631
CRYST1 82.760 133.895 118.886 90.00 104.95 90.00 P 1 21 1 12
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 0.012083 0.000000 0.003226 0.00000
SCALE2 0.000000 0.007469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008706 0.00000
TER 2539 TYR A 353
TER 5023 LEU B 352
TER 7384 ASN C 351
TER 9835 TYR D 353
TER 12228 LEU E 352
TER 14603 TYR F 353
MASTER 801 0 32 67 54 0 60 616004 6 274 174
END
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