HEADER LYASE 31-DEC-02 1NJJ
TITLE CRYSTAL STRUCTURE DETERMINATION OF T. BRUCEI ORNITHINE DECARBOXYLASE
TITLE 2 BOUND TO D-ORNITHINE AND TO G418
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORNITHINE DECARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.1.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI GAMBIENSE;
SOURCE 3 ORGANISM_TAXID: 31285;
SOURCE 4 STRAIN: GAMBIENSE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PODC29
KEYWDS ORNITHINE DECARBOXYLASE, ODC, PLP, PYRIDOXAL 5'-PHOSPHATE, D-
KEYWDS 2 ORNITHINE, G418, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.K.JACKSON,E.J.GOLDSMITH,M.A.PHILLIPS
REVDAT 4 16-AUG-23 1NJJ 1 REMARK
REVDAT 3 31-JAN-18 1NJJ 1 REMARK
REVDAT 2 24-FEB-09 1NJJ 1 VERSN
REVDAT 1 26-AUG-03 1NJJ 0
JRNL AUTH L.K.JACKSON,E.J.GOLDSMITH,M.A.PHILLIPS
JRNL TITL X-RAY STRUCTURE DETERMINATION OF TRYPANOSOMA BRUCEI
JRNL TITL 2 ORNITHINE DECARBOXYLASE BOUND TO D-ORNITHINE AND TO G418:
JRNL TITL 3 INSIGHTS INTO SUBSTRATE BINDING AND ODC CONFORMATIONAL
JRNL TITL 4 FLEXIBILITY.
JRNL REF J.BIOL.CHEM. V. 278 22037 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12672797
JRNL DOI 10.1074/JBC.M300188200
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 49323
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4953
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 297
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11019
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.10
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017922.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 98.5
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63372
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1F3T WITH WATERS, K69, C360 AND
REMARK 200 PUTRESCINE REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, HEPES, DTT, NACL, D
REMARK 280 -ORNITHINE, G418, BUTYROLACTONE, PH 7, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 16K, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.27000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 1
REMARK 465 SER A 2
REMARK 465 MET A 3
REMARK 465 ASP A 4
REMARK 465 ILE A 5
REMARK 465 VAL A 6
REMARK 465 VAL A 7
REMARK 465 ASN A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 CYS A 13
REMARK 465 ARG A 14
REMARK 465 PHE A 15
REMARK 465 LEU A 16
REMARK 465 GLU A 17
REMARK 465 GLY A 18
REMARK 465 PHE A 19
REMARK 465 ILE A 29
REMARK 465 SER A 30
REMARK 465 MET A 31
REMARK 465 ASN A 32
REMARK 465 THR A 33
REMARK 465 CYS A 34
REMARK 465 ASP A 35
REMARK 465 GLU A 36
REMARK 465 ASP A 158
REMARK 465 ASP A 159
REMARK 465 SER A 160
REMARK 465 LEU A 161
REMARK 465 ALA A 162
REMARK 465 ARG A 163
REMARK 465 CYS A 164
REMARK 465 ARG A 165
REMARK 465 LEU A 166
REMARK 465 SER A 167
REMARK 465 PRO A 297
REMARK 465 GLY A 298
REMARK 465 VAL A 299
REMARK 465 GLN A 300
REMARK 465 THR A 301
REMARK 465 ASP A 302
REMARK 465 VAL A 303
REMARK 465 GLY A 304
REMARK 465 ALA A 305
REMARK 465 HIS A 306
REMARK 465 ALA A 307
REMARK 465 GLU A 308
REMARK 465 SER A 309
REMARK 465 ASN A 310
REMARK 465 ALA A 311
REMARK 465 ILE A 345
REMARK 465 PRO A 346
REMARK 465 ASN A 347
REMARK 465 VAL A 392
REMARK 465 GLY A 393
REMARK 465 THR A 394
REMARK 465 SER A 395
REMARK 465 SER A 396
REMARK 465 PHE A 397
REMARK 465 ASN A 398
REMARK 465 GLY A 399
REMARK 465 PHE A 400
REMARK 465 GLN A 401
REMARK 465 HIS A 415
REMARK 465 VAL A 416
REMARK 465 VAL A 417
REMARK 465 ARG A 418
REMARK 465 GLU A 419
REMARK 465 LEU A 420
REMARK 465 LYS A 421
REMARK 465 SER A 422
REMARK 465 GLN A 423
REMARK 465 LYS A 424
REMARK 465 SER A 425
REMARK 465 LYS B 1
REMARK 465 SER B 2
REMARK 465 MET B 3
REMARK 465 ASP B 4
REMARK 465 ILE B 5
REMARK 465 VAL B 6
REMARK 465 VAL B 7
REMARK 465 ASN B 8
REMARK 465 ASP B 9
REMARK 465 ASP B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 CYS B 13
REMARK 465 ARG B 14
REMARK 465 PHE B 15
REMARK 465 LEU B 16
REMARK 465 GLU B 17
REMARK 465 GLY B 18
REMARK 465 PHE B 19
REMARK 465 MET B 31
REMARK 465 ASN B 32
REMARK 465 THR B 33
REMARK 465 CYS B 34
REMARK 465 ASP B 35
REMARK 465 GLU B 36
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 LEU B 161
REMARK 465 ALA B 162
REMARK 465 ARG B 163
REMARK 465 CYS B 164
REMARK 465 ARG B 165
REMARK 465 LEU B 166
REMARK 465 SER B 167
REMARK 465 PRO B 297
REMARK 465 GLY B 298
REMARK 465 VAL B 299
REMARK 465 GLN B 300
REMARK 465 THR B 301
REMARK 465 ASP B 302
REMARK 465 VAL B 303
REMARK 465 GLY B 304
REMARK 465 ALA B 305
REMARK 465 HIS B 306
REMARK 465 ALA B 307
REMARK 465 GLU B 308
REMARK 465 SER B 309
REMARK 465 ASN B 310
REMARK 465 ALA B 311
REMARK 465 VAL B 392
REMARK 465 GLY B 393
REMARK 465 THR B 394
REMARK 465 SER B 395
REMARK 465 SER B 396
REMARK 465 PHE B 397
REMARK 465 ASN B 398
REMARK 465 GLY B 399
REMARK 465 PHE B 400
REMARK 465 GLN B 401
REMARK 465 SER B 410
REMARK 465 GLY B 411
REMARK 465 LEU B 412
REMARK 465 PRO B 413
REMARK 465 ASP B 414
REMARK 465 HIS B 415
REMARK 465 VAL B 416
REMARK 465 VAL B 417
REMARK 465 ARG B 418
REMARK 465 GLU B 419
REMARK 465 LEU B 420
REMARK 465 LYS B 421
REMARK 465 SER B 422
REMARK 465 GLN B 423
REMARK 465 LYS B 424
REMARK 465 SER B 425
REMARK 465 LYS C 1
REMARK 465 SER C 2
REMARK 465 MET C 3
REMARK 465 ASP C 4
REMARK 465 ILE C 5
REMARK 465 VAL C 6
REMARK 465 VAL C 7
REMARK 465 ASN C 8
REMARK 465 ASP C 9
REMARK 465 ASP C 10
REMARK 465 LEU C 11
REMARK 465 SER C 12
REMARK 465 CYS C 13
REMARK 465 ILE C 29
REMARK 465 SER C 30
REMARK 465 MET C 31
REMARK 465 ASN C 32
REMARK 465 THR C 33
REMARK 465 CYS C 34
REMARK 465 ASP C 35
REMARK 465 GLU C 36
REMARK 465 ASP C 158
REMARK 465 ASP C 159
REMARK 465 SER C 160
REMARK 465 LEU C 161
REMARK 465 ALA C 162
REMARK 465 ARG C 163
REMARK 465 CYS C 164
REMARK 465 ARG C 165
REMARK 465 LEU C 166
REMARK 465 SER C 167
REMARK 465 PRO C 297
REMARK 465 GLY C 298
REMARK 465 VAL C 299
REMARK 465 GLN C 300
REMARK 465 THR C 301
REMARK 465 ASP C 302
REMARK 465 VAL C 303
REMARK 465 GLY C 304
REMARK 465 ALA C 305
REMARK 465 HIS C 306
REMARK 465 ALA C 307
REMARK 465 GLU C 308
REMARK 465 SER C 309
REMARK 465 ASN C 310
REMARK 465 ALA C 311
REMARK 465 PRO C 346
REMARK 465 ASN C 347
REMARK 465 GLY C 393
REMARK 465 THR C 394
REMARK 465 SER C 395
REMARK 465 SER C 396
REMARK 465 PHE C 397
REMARK 465 ASN C 398
REMARK 465 GLY C 399
REMARK 465 PHE C 400
REMARK 465 GLN C 401
REMARK 465 SER C 410
REMARK 465 GLY C 411
REMARK 465 LEU C 412
REMARK 465 PRO C 413
REMARK 465 ASP C 414
REMARK 465 HIS C 415
REMARK 465 VAL C 416
REMARK 465 VAL C 417
REMARK 465 ARG C 418
REMARK 465 GLU C 419
REMARK 465 LEU C 420
REMARK 465 LYS C 421
REMARK 465 SER C 422
REMARK 465 GLN C 423
REMARK 465 LYS C 424
REMARK 465 SER C 425
REMARK 465 LYS D 1
REMARK 465 SER D 2
REMARK 465 MET D 3
REMARK 465 ASP D 4
REMARK 465 ILE D 5
REMARK 465 VAL D 6
REMARK 465 VAL D 7
REMARK 465 ASN D 8
REMARK 465 ASP D 9
REMARK 465 ASP D 10
REMARK 465 LEU D 11
REMARK 465 SER D 12
REMARK 465 CYS D 13
REMARK 465 ARG D 14
REMARK 465 PHE D 15
REMARK 465 LEU D 16
REMARK 465 GLU D 17
REMARK 465 GLY D 18
REMARK 465 PHE D 19
REMARK 465 MET D 31
REMARK 465 ASN D 32
REMARK 465 THR D 33
REMARK 465 CYS D 34
REMARK 465 ASP D 35
REMARK 465 GLU D 36
REMARK 465 ASP D 158
REMARK 465 ASP D 159
REMARK 465 SER D 160
REMARK 465 LEU D 161
REMARK 465 ALA D 162
REMARK 465 ARG D 163
REMARK 465 CYS D 164
REMARK 465 ARG D 165
REMARK 465 LEU D 166
REMARK 465 SER D 167
REMARK 465 PRO D 297
REMARK 465 GLY D 298
REMARK 465 VAL D 299
REMARK 465 GLN D 300
REMARK 465 THR D 301
REMARK 465 ASP D 302
REMARK 465 VAL D 303
REMARK 465 GLY D 304
REMARK 465 ALA D 305
REMARK 465 HIS D 306
REMARK 465 ALA D 307
REMARK 465 GLU D 308
REMARK 465 VAL D 392
REMARK 465 GLY D 393
REMARK 465 THR D 394
REMARK 465 SER D 395
REMARK 465 SER D 396
REMARK 465 PHE D 397
REMARK 465 ASN D 398
REMARK 465 GLY D 399
REMARK 465 SER D 410
REMARK 465 GLY D 411
REMARK 465 LEU D 412
REMARK 465 PRO D 413
REMARK 465 ASP D 414
REMARK 465 HIS D 415
REMARK 465 VAL D 416
REMARK 465 VAL D 417
REMARK 465 ARG D 418
REMARK 465 GLU D 419
REMARK 465 LEU D 420
REMARK 465 LYS D 421
REMARK 465 SER D 422
REMARK 465 GLN D 423
REMARK 465 LYS D 424
REMARK 465 SER D 425
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 PHE D 400 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 GLN D 401 CB CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 61 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP A 137 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 204 CB - CG - OD1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG A 337 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 337 NE - CZ - NH1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 337 NE - CZ - NH2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 PRO A 344 C - N - CA ANGL. DEV. = 14.1 DEGREES
REMARK 500 PRO A 344 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 PRO A 413 C - N - CA ANGL. DEV. = 12.3 DEGREES
REMARK 500 LEU B 25 CB - CA - C ANGL. DEV. = -13.4 DEGREES
REMARK 500 LYS B 27 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 137 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP B 204 CB - CG - OD1 ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG B 337 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG B 337 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 337 NE - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 PRO B 344 C - N - CA ANGL. DEV. = 13.8 DEGREES
REMARK 500 PRO B 344 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO B 403 N - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG C 337 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG C 337 NE - CZ - NH1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG C 337 NE - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP D 137 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 ASP D 137 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 GLN D 312 N - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 ARG D 337 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 VAL D 391 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 PRO D 403 C - N - CA ANGL. DEV. = -10.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 22 4.51 -46.53
REMARK 500 ASP A 23 26.15 -154.84
REMARK 500 LEU A 25 -79.40 -56.81
REMARK 500 CYS A 26 -8.97 -47.86
REMARK 500 ALA A 67 87.47 -67.67
REMARK 500 ASN A 71 111.99 -171.27
REMARK 500 ASP A 134 14.54 -146.40
REMARK 500 LYS A 148 32.83 -82.81
REMARK 500 PRO A 264 150.53 -49.92
REMARK 500 ASP A 266 123.34 -173.48
REMARK 500 GLU A 274 68.59 -119.20
REMARK 500 ASN A 319 41.82 -81.94
REMARK 500 ASP A 320 144.48 -172.51
REMARK 500 GLN A 341 44.18 -101.60
REMARK 500 GLU A 368 -62.01 -93.10
REMARK 500 THR A 390 -30.46 -132.89
REMARK 500 PRO A 403 117.65 -26.90
REMARK 500 PRO A 413 77.06 -58.73
REMARK 500 ARG B 22 -6.71 -53.00
REMARK 500 CYS B 26 47.71 -94.86
REMARK 500 LYS B 27 -58.40 -144.74
REMARK 500 ILE B 29 58.34 -93.29
REMARK 500 ALA B 67 87.14 -68.41
REMARK 500 ASN B 71 111.71 -171.66
REMARK 500 ASP B 134 14.87 -147.55
REMARK 500 LYS B 148 32.25 -82.13
REMARK 500 PRO B 264 150.02 -49.96
REMARK 500 ASP B 266 124.63 -173.31
REMARK 500 GLU B 274 67.77 -119.75
REMARK 500 ASN B 319 40.94 -82.45
REMARK 500 ASP B 320 145.02 -171.44
REMARK 500 GLU B 343 150.24 -46.10
REMARK 500 PRO B 344 174.52 -54.21
REMARK 500 ILE B 345 -96.46 -129.91
REMARK 500 PRO B 346 -106.83 -113.99
REMARK 500 GLU B 348 143.60 -36.73
REMARK 500 GLU B 368 -61.23 -93.06
REMARK 500 PHE C 19 -2.69 -160.10
REMARK 500 LYS C 27 87.07 -35.02
REMARK 500 ALA C 67 87.07 -69.33
REMARK 500 ASN C 71 112.03 -172.34
REMARK 500 ASP C 134 14.02 -146.66
REMARK 500 LYS C 148 31.94 -82.80
REMARK 500 ARG C 242 43.76 -81.60
REMARK 500 PRO C 264 150.03 -49.74
REMARK 500 ASP C 266 123.52 -172.71
REMARK 500 GLU C 274 69.26 -119.54
REMARK 500 ASN C 319 41.12 -82.09
REMARK 500 ASP C 320 144.30 -171.53
REMARK 500 PRO C 344 -171.26 -51.92
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
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 GET A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GET B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GET C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORX A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORX B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORX C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORX D 426
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QU4 RELATED DB: PDB
REMARK 900 NATIVE T. BRUCEI ORNITHINE DECARBOXYLASE
REMARK 900 RELATED ID: 1F3T RELATED DB: PDB
REMARK 900 T. BRUCEI ORNITHINE DECARBOXYLASE COMPLEXED WITH PRODUCT PUTRESCINE
DBREF 1NJJ A 1 425 UNP Q9TZZ6 Q9TZZ6_TRYBG 21 445
DBREF 1NJJ B 1 425 UNP Q9TZZ6 Q9TZZ6_TRYBG 21 445
DBREF 1NJJ C 1 425 UNP Q9TZZ6 Q9TZZ6_TRYBG 21 445
DBREF 1NJJ D 1 425 UNP Q9TZZ6 Q9TZZ6_TRYBG 21 445
SEQRES 1 A 425 LYS SER MET ASP ILE VAL VAL ASN ASP ASP LEU SER CYS
SEQRES 2 A 425 ARG PHE LEU GLU GLY PHE ASN THR ARG ASP ALA LEU CYS
SEQRES 3 A 425 LYS LYS ILE SER MET ASN THR CYS ASP GLU GLY ASP PRO
SEQRES 4 A 425 PHE PHE VAL ALA ASP LEU GLY ASP ILE VAL ARG LYS HIS
SEQRES 5 A 425 GLU THR TRP LYS LYS CYS LEU PRO ARG VAL THR PRO PHE
SEQRES 6 A 425 TYR ALA VAL LYS CYS ASN ASP ASP TRP ARG VAL LEU GLY
SEQRES 7 A 425 THR LEU ALA ALA LEU GLY THR GLY PHE ASP CYS ALA SER
SEQRES 8 A 425 ASN THR GLU ILE GLN ARG VAL ARG GLY ILE GLY VAL PRO
SEQRES 9 A 425 PRO GLU LYS ILE ILE TYR ALA ASN PRO CYS LYS GLN ILE
SEQRES 10 A 425 SER HIS ILE ARG TYR ALA ARG ASP SER GLY VAL ASP VAL
SEQRES 11 A 425 MET THR PHE ASP CYS VAL ASP GLU LEU GLU LYS VAL ALA
SEQRES 12 A 425 LYS THR HIS PRO LYS ALA LYS MET VAL LEU ARG ILE SER
SEQRES 13 A 425 THR ASP ASP SER LEU ALA ARG CYS ARG LEU SER VAL LYS
SEQRES 14 A 425 PHE GLY ALA LYS VAL GLU ASP CYS ARG PHE ILE LEU GLU
SEQRES 15 A 425 GLN ALA LYS LYS LEU ASN ILE ASP VAL THR GLY VAL SER
SEQRES 16 A 425 PHE HIS VAL GLY SER GLY SER THR ASP ALA SER THR PHE
SEQRES 17 A 425 ALA GLN ALA ILE SER ASP SER ARG PHE VAL PHE ASP MET
SEQRES 18 A 425 GLY THR GLU LEU GLY PHE ASN MET HIS ILE LEU ASP ILE
SEQRES 19 A 425 GLY GLY GLY PHE PRO GLY THR ARG ASP ALA PRO LEU LYS
SEQRES 20 A 425 PHE GLU GLU ILE ALA GLY VAL ILE ASN ASN ALA LEU GLU
SEQRES 21 A 425 LYS HIS PHE PRO PRO ASP LEU LYS LEU THR ILE VAL ALA
SEQRES 22 A 425 GLU PRO GLY ARG TYR TYR VAL ALA SER ALA PHE THR LEU
SEQRES 23 A 425 ALA VAL ASN VAL ILE ALA LYS LYS VAL THR PRO GLY VAL
SEQRES 24 A 425 GLN THR ASP VAL GLY ALA HIS ALA GLU SER ASN ALA GLN
SEQRES 25 A 425 SER PHE MET TYR TYR VAL ASN ASP GLY VAL TYR GLY SER
SEQRES 26 A 425 PHE ASN CYS ILE LEU TYR ASP HIS ALA VAL VAL ARG PRO
SEQRES 27 A 425 LEU PRO GLN ARG GLU PRO ILE PRO ASN GLU LYS LEU TYR
SEQRES 28 A 425 PRO SER SER VAL TRP GLY PRO THR CYS ASP GLY LEU ASP
SEQRES 29 A 425 GLN ILE VAL GLU ARG TYR TYR LEU PRO GLU MET GLN VAL
SEQRES 30 A 425 GLY GLU TRP LEU LEU PHE GLU ASP MET GLY ALA TYR THR
SEQRES 31 A 425 VAL VAL GLY THR SER SER PHE ASN GLY PHE GLN SER PRO
SEQRES 32 A 425 THR ILE TYR TYR VAL VAL SER GLY LEU PRO ASP HIS VAL
SEQRES 33 A 425 VAL ARG GLU LEU LYS SER GLN LYS SER
SEQRES 1 B 425 LYS SER MET ASP ILE VAL VAL ASN ASP ASP LEU SER CYS
SEQRES 2 B 425 ARG PHE LEU GLU GLY PHE ASN THR ARG ASP ALA LEU CYS
SEQRES 3 B 425 LYS LYS ILE SER MET ASN THR CYS ASP GLU GLY ASP PRO
SEQRES 4 B 425 PHE PHE VAL ALA ASP LEU GLY ASP ILE VAL ARG LYS HIS
SEQRES 5 B 425 GLU THR TRP LYS LYS CYS LEU PRO ARG VAL THR PRO PHE
SEQRES 6 B 425 TYR ALA VAL LYS CYS ASN ASP ASP TRP ARG VAL LEU GLY
SEQRES 7 B 425 THR LEU ALA ALA LEU GLY THR GLY PHE ASP CYS ALA SER
SEQRES 8 B 425 ASN THR GLU ILE GLN ARG VAL ARG GLY ILE GLY VAL PRO
SEQRES 9 B 425 PRO GLU LYS ILE ILE TYR ALA ASN PRO CYS LYS GLN ILE
SEQRES 10 B 425 SER HIS ILE ARG TYR ALA ARG ASP SER GLY VAL ASP VAL
SEQRES 11 B 425 MET THR PHE ASP CYS VAL ASP GLU LEU GLU LYS VAL ALA
SEQRES 12 B 425 LYS THR HIS PRO LYS ALA LYS MET VAL LEU ARG ILE SER
SEQRES 13 B 425 THR ASP ASP SER LEU ALA ARG CYS ARG LEU SER VAL LYS
SEQRES 14 B 425 PHE GLY ALA LYS VAL GLU ASP CYS ARG PHE ILE LEU GLU
SEQRES 15 B 425 GLN ALA LYS LYS LEU ASN ILE ASP VAL THR GLY VAL SER
SEQRES 16 B 425 PHE HIS VAL GLY SER GLY SER THR ASP ALA SER THR PHE
SEQRES 17 B 425 ALA GLN ALA ILE SER ASP SER ARG PHE VAL PHE ASP MET
SEQRES 18 B 425 GLY THR GLU LEU GLY PHE ASN MET HIS ILE LEU ASP ILE
SEQRES 19 B 425 GLY GLY GLY PHE PRO GLY THR ARG ASP ALA PRO LEU LYS
SEQRES 20 B 425 PHE GLU GLU ILE ALA GLY VAL ILE ASN ASN ALA LEU GLU
SEQRES 21 B 425 LYS HIS PHE PRO PRO ASP LEU LYS LEU THR ILE VAL ALA
SEQRES 22 B 425 GLU PRO GLY ARG TYR TYR VAL ALA SER ALA PHE THR LEU
SEQRES 23 B 425 ALA VAL ASN VAL ILE ALA LYS LYS VAL THR PRO GLY VAL
SEQRES 24 B 425 GLN THR ASP VAL GLY ALA HIS ALA GLU SER ASN ALA GLN
SEQRES 25 B 425 SER PHE MET TYR TYR VAL ASN ASP GLY VAL TYR GLY SER
SEQRES 26 B 425 PHE ASN CYS ILE LEU TYR ASP HIS ALA VAL VAL ARG PRO
SEQRES 27 B 425 LEU PRO GLN ARG GLU PRO ILE PRO ASN GLU LYS LEU TYR
SEQRES 28 B 425 PRO SER SER VAL TRP GLY PRO THR CYS ASP GLY LEU ASP
SEQRES 29 B 425 GLN ILE VAL GLU ARG TYR TYR LEU PRO GLU MET GLN VAL
SEQRES 30 B 425 GLY GLU TRP LEU LEU PHE GLU ASP MET GLY ALA TYR THR
SEQRES 31 B 425 VAL VAL GLY THR SER SER PHE ASN GLY PHE GLN SER PRO
SEQRES 32 B 425 THR ILE TYR TYR VAL VAL SER GLY LEU PRO ASP HIS VAL
SEQRES 33 B 425 VAL ARG GLU LEU LYS SER GLN LYS SER
SEQRES 1 C 425 LYS SER MET ASP ILE VAL VAL ASN ASP ASP LEU SER CYS
SEQRES 2 C 425 ARG PHE LEU GLU GLY PHE ASN THR ARG ASP ALA LEU CYS
SEQRES 3 C 425 LYS LYS ILE SER MET ASN THR CYS ASP GLU GLY ASP PRO
SEQRES 4 C 425 PHE PHE VAL ALA ASP LEU GLY ASP ILE VAL ARG LYS HIS
SEQRES 5 C 425 GLU THR TRP LYS LYS CYS LEU PRO ARG VAL THR PRO PHE
SEQRES 6 C 425 TYR ALA VAL LYS CYS ASN ASP ASP TRP ARG VAL LEU GLY
SEQRES 7 C 425 THR LEU ALA ALA LEU GLY THR GLY PHE ASP CYS ALA SER
SEQRES 8 C 425 ASN THR GLU ILE GLN ARG VAL ARG GLY ILE GLY VAL PRO
SEQRES 9 C 425 PRO GLU LYS ILE ILE TYR ALA ASN PRO CYS LYS GLN ILE
SEQRES 10 C 425 SER HIS ILE ARG TYR ALA ARG ASP SER GLY VAL ASP VAL
SEQRES 11 C 425 MET THR PHE ASP CYS VAL ASP GLU LEU GLU LYS VAL ALA
SEQRES 12 C 425 LYS THR HIS PRO LYS ALA LYS MET VAL LEU ARG ILE SER
SEQRES 13 C 425 THR ASP ASP SER LEU ALA ARG CYS ARG LEU SER VAL LYS
SEQRES 14 C 425 PHE GLY ALA LYS VAL GLU ASP CYS ARG PHE ILE LEU GLU
SEQRES 15 C 425 GLN ALA LYS LYS LEU ASN ILE ASP VAL THR GLY VAL SER
SEQRES 16 C 425 PHE HIS VAL GLY SER GLY SER THR ASP ALA SER THR PHE
SEQRES 17 C 425 ALA GLN ALA ILE SER ASP SER ARG PHE VAL PHE ASP MET
SEQRES 18 C 425 GLY THR GLU LEU GLY PHE ASN MET HIS ILE LEU ASP ILE
SEQRES 19 C 425 GLY GLY GLY PHE PRO GLY THR ARG ASP ALA PRO LEU LYS
SEQRES 20 C 425 PHE GLU GLU ILE ALA GLY VAL ILE ASN ASN ALA LEU GLU
SEQRES 21 C 425 LYS HIS PHE PRO PRO ASP LEU LYS LEU THR ILE VAL ALA
SEQRES 22 C 425 GLU PRO GLY ARG TYR TYR VAL ALA SER ALA PHE THR LEU
SEQRES 23 C 425 ALA VAL ASN VAL ILE ALA LYS LYS VAL THR PRO GLY VAL
SEQRES 24 C 425 GLN THR ASP VAL GLY ALA HIS ALA GLU SER ASN ALA GLN
SEQRES 25 C 425 SER PHE MET TYR TYR VAL ASN ASP GLY VAL TYR GLY SER
SEQRES 26 C 425 PHE ASN CYS ILE LEU TYR ASP HIS ALA VAL VAL ARG PRO
SEQRES 27 C 425 LEU PRO GLN ARG GLU PRO ILE PRO ASN GLU LYS LEU TYR
SEQRES 28 C 425 PRO SER SER VAL TRP GLY PRO THR CYS ASP GLY LEU ASP
SEQRES 29 C 425 GLN ILE VAL GLU ARG TYR TYR LEU PRO GLU MET GLN VAL
SEQRES 30 C 425 GLY GLU TRP LEU LEU PHE GLU ASP MET GLY ALA TYR THR
SEQRES 31 C 425 VAL VAL GLY THR SER SER PHE ASN GLY PHE GLN SER PRO
SEQRES 32 C 425 THR ILE TYR TYR VAL VAL SER GLY LEU PRO ASP HIS VAL
SEQRES 33 C 425 VAL ARG GLU LEU LYS SER GLN LYS SER
SEQRES 1 D 425 LYS SER MET ASP ILE VAL VAL ASN ASP ASP LEU SER CYS
SEQRES 2 D 425 ARG PHE LEU GLU GLY PHE ASN THR ARG ASP ALA LEU CYS
SEQRES 3 D 425 LYS LYS ILE SER MET ASN THR CYS ASP GLU GLY ASP PRO
SEQRES 4 D 425 PHE PHE VAL ALA ASP LEU GLY ASP ILE VAL ARG LYS HIS
SEQRES 5 D 425 GLU THR TRP LYS LYS CYS LEU PRO ARG VAL THR PRO PHE
SEQRES 6 D 425 TYR ALA VAL LYS CYS ASN ASP ASP TRP ARG VAL LEU GLY
SEQRES 7 D 425 THR LEU ALA ALA LEU GLY THR GLY PHE ASP CYS ALA SER
SEQRES 8 D 425 ASN THR GLU ILE GLN ARG VAL ARG GLY ILE GLY VAL PRO
SEQRES 9 D 425 PRO GLU LYS ILE ILE TYR ALA ASN PRO CYS LYS GLN ILE
SEQRES 10 D 425 SER HIS ILE ARG TYR ALA ARG ASP SER GLY VAL ASP VAL
SEQRES 11 D 425 MET THR PHE ASP CYS VAL ASP GLU LEU GLU LYS VAL ALA
SEQRES 12 D 425 LYS THR HIS PRO LYS ALA LYS MET VAL LEU ARG ILE SER
SEQRES 13 D 425 THR ASP ASP SER LEU ALA ARG CYS ARG LEU SER VAL LYS
SEQRES 14 D 425 PHE GLY ALA LYS VAL GLU ASP CYS ARG PHE ILE LEU GLU
SEQRES 15 D 425 GLN ALA LYS LYS LEU ASN ILE ASP VAL THR GLY VAL SER
SEQRES 16 D 425 PHE HIS VAL GLY SER GLY SER THR ASP ALA SER THR PHE
SEQRES 17 D 425 ALA GLN ALA ILE SER ASP SER ARG PHE VAL PHE ASP MET
SEQRES 18 D 425 GLY THR GLU LEU GLY PHE ASN MET HIS ILE LEU ASP ILE
SEQRES 19 D 425 GLY GLY GLY PHE PRO GLY THR ARG ASP ALA PRO LEU LYS
SEQRES 20 D 425 PHE GLU GLU ILE ALA GLY VAL ILE ASN ASN ALA LEU GLU
SEQRES 21 D 425 LYS HIS PHE PRO PRO ASP LEU LYS LEU THR ILE VAL ALA
SEQRES 22 D 425 GLU PRO GLY ARG TYR TYR VAL ALA SER ALA PHE THR LEU
SEQRES 23 D 425 ALA VAL ASN VAL ILE ALA LYS LYS VAL THR PRO GLY VAL
SEQRES 24 D 425 GLN THR ASP VAL GLY ALA HIS ALA GLU SER ASN ALA GLN
SEQRES 25 D 425 SER PHE MET TYR TYR VAL ASN ASP GLY VAL TYR GLY SER
SEQRES 26 D 425 PHE ASN CYS ILE LEU TYR ASP HIS ALA VAL VAL ARG PRO
SEQRES 27 D 425 LEU PRO GLN ARG GLU PRO ILE PRO ASN GLU LYS LEU TYR
SEQRES 28 D 425 PRO SER SER VAL TRP GLY PRO THR CYS ASP GLY LEU ASP
SEQRES 29 D 425 GLN ILE VAL GLU ARG TYR TYR LEU PRO GLU MET GLN VAL
SEQRES 30 D 425 GLY GLU TRP LEU LEU PHE GLU ASP MET GLY ALA TYR THR
SEQRES 31 D 425 VAL VAL GLY THR SER SER PHE ASN GLY PHE GLN SER PRO
SEQRES 32 D 425 THR ILE TYR TYR VAL VAL SER GLY LEU PRO ASP HIS VAL
SEQRES 33 D 425 VAL ARG GLU LEU LYS SER GLN LYS SER
HET GET A 601 34
HET ORX A 602 24
HET GET B 602 34
HET ORX B 603 24
HET GET C 603 34
HET ORX C 604 24
HET ORX D 426 24
HETNAM GET GENETICIN
HETNAM ORX N~2~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 ORX METHYL]PYRIDIN-4-YL}METHYL)-D-ORNITHINE
HETSYN GET G418
FORMUL 5 GET 3(C20 H40 N4 O10)
FORMUL 6 ORX 4(C13 H22 N3 O7 P)
FORMUL 12 HOH *207(H2 O)
HELIX 1 1 LEU A 45 LEU A 59 1 15
HELIX 2 2 LYS A 69 ASN A 71 5 3
HELIX 3 3 ASP A 73 LEU A 83 1 11
HELIX 4 4 SER A 91 ILE A 101 1 11
HELIX 5 5 PRO A 104 GLU A 106 5 3
HELIX 6 6 GLN A 116 SER A 126 1 11
HELIX 7 7 CYS A 135 HIS A 146 1 12
HELIX 8 8 LYS A 173 GLU A 175 5 3
HELIX 9 9 ASP A 176 LEU A 187 1 12
HELIX 10 10 ALA A 205 LEU A 225 1 21
HELIX 11 11 LYS A 247 PHE A 263 1 17
HELIX 12 12 GLY A 276 ALA A 281 1 6
HELIX 13 13 GLY A 324 PHE A 326 5 3
HELIX 14 14 ASN A 327 ASP A 332 1 6
HELIX 15 15 ASN B 20 LEU B 25 1 6
HELIX 16 16 LEU B 45 LEU B 59 1 15
HELIX 17 17 LYS B 69 ASN B 71 5 3
HELIX 18 18 ASP B 73 LEU B 83 1 11
HELIX 19 19 SER B 91 ILE B 101 1 11
HELIX 20 20 PRO B 104 GLU B 106 5 3
HELIX 21 21 GLN B 116 SER B 126 1 11
HELIX 22 22 CYS B 135 HIS B 146 1 12
HELIX 23 23 LYS B 173 GLU B 175 5 3
HELIX 24 24 ASP B 176 LEU B 187 1 12
HELIX 25 25 ALA B 205 LEU B 225 1 21
HELIX 26 26 LYS B 247 PHE B 263 1 17
HELIX 27 27 GLY B 276 ALA B 281 1 6
HELIX 28 28 GLY B 324 PHE B 326 5 3
HELIX 29 29 ASN B 327 ASP B 332 1 6
HELIX 30 30 THR C 21 LYS C 27 1 7
HELIX 31 31 LEU C 45 LEU C 59 1 15
HELIX 32 32 LYS C 69 ASN C 71 5 3
HELIX 33 33 ASP C 73 LEU C 83 1 11
HELIX 34 34 SER C 91 ILE C 101 1 11
HELIX 35 35 PRO C 104 GLU C 106 5 3
HELIX 36 36 GLN C 116 SER C 126 1 11
HELIX 37 37 CYS C 135 HIS C 146 1 12
HELIX 38 38 LYS C 173 GLU C 175 5 3
HELIX 39 39 ASP C 176 LEU C 187 1 12
HELIX 40 40 ALA C 205 LEU C 225 1 21
HELIX 41 41 LYS C 247 PHE C 263 1 17
HELIX 42 42 GLY C 276 ALA C 281 1 6
HELIX 43 43 GLY C 324 PHE C 326 5 3
HELIX 44 44 ASN C 327 ASP C 332 1 6
HELIX 45 45 ASN D 20 ASP D 23 5 4
HELIX 46 46 ALA D 24 ILE D 29 1 6
HELIX 47 47 LEU D 45 LEU D 59 1 15
HELIX 48 48 LYS D 69 ASN D 71 5 3
HELIX 49 49 ASP D 73 LEU D 83 1 11
HELIX 50 50 SER D 91 ILE D 101 1 11
HELIX 51 51 PRO D 104 GLU D 106 5 3
HELIX 52 52 GLN D 116 SER D 126 1 11
HELIX 53 53 CYS D 135 HIS D 146 1 12
HELIX 54 54 LYS D 173 GLU D 175 5 3
HELIX 55 55 ASP D 176 LEU D 187 1 12
HELIX 56 56 ALA D 205 LEU D 225 1 21
HELIX 57 57 LYS D 247 PHE D 263 1 17
HELIX 58 58 GLY D 276 ALA D 281 1 6
HELIX 59 59 GLY D 324 PHE D 326 5 3
HELIX 60 60 ASN D 327 ASP D 332 1 6
SHEET 1 A 6 GLN A 365 PRO A 373 0
SHEET 2 A 6 LEU A 350 TRP A 356 -1 N TYR A 351 O LEU A 372
SHEET 3 A 6 PHE A 314 VAL A 318 1 N TYR A 316 O SER A 354
SHEET 4 A 6 PHE A 284 VAL A 295 -1 N ALA A 292 O TYR A 317
SHEET 5 A 6 PHE A 40 ASP A 44 -1 N PHE A 40 O ALA A 287
SHEET 6 A 6 THR A 404 VAL A 408 1 O TYR A 406 N ALA A 43
SHEET 1 B 6 GLN A 365 PRO A 373 0
SHEET 2 B 6 LEU A 350 TRP A 356 -1 N TYR A 351 O LEU A 372
SHEET 3 B 6 PHE A 314 VAL A 318 1 N TYR A 316 O SER A 354
SHEET 4 B 6 PHE A 284 VAL A 295 -1 N ALA A 292 O TYR A 317
SHEET 5 B 6 TRP A 380 GLU A 384 -1 O PHE A 383 N LEU A 286
SHEET 6 B 6 PRO A 338 PRO A 340 -1 N LEU A 339 O LEU A 382
SHEET 1 C 9 VAL A 62 ALA A 67 0
SHEET 2 C 9 GLY A 86 CYS A 89 1 O GLY A 86 N TYR A 66
SHEET 3 C 9 ILE A 108 TYR A 110 1 O ILE A 109 N PHE A 87
SHEET 4 C 9 VAL A 130 PHE A 133 1 O VAL A 130 N TYR A 110
SHEET 5 C 9 LYS A 150 ARG A 154 1 O VAL A 152 N MET A 131
SHEET 6 C 9 VAL A 191 SER A 195 1 O GLY A 193 N LEU A 153
SHEET 7 C 9 ILE A 231 ASP A 233 1 O ASP A 233 N VAL A 194
SHEET 8 C 9 THR A 270 ALA A 273 1 O VAL A 272 N LEU A 232
SHEET 9 C 9 VAL A 62 ALA A 67 1 N THR A 63 O ILE A 271
SHEET 1 D 6 GLN B 365 PRO B 373 0
SHEET 2 D 6 LEU B 350 TRP B 356 -1 N TYR B 351 O LEU B 372
SHEET 3 D 6 PHE B 314 VAL B 318 1 N TYR B 316 O SER B 354
SHEET 4 D 6 PHE B 284 VAL B 295 -1 N ALA B 292 O TYR B 317
SHEET 5 D 6 PHE B 40 ASP B 44 -1 N PHE B 40 O ALA B 287
SHEET 6 D 6 THR B 404 VAL B 408 1 O TYR B 406 N ALA B 43
SHEET 1 E 6 GLN B 365 PRO B 373 0
SHEET 2 E 6 LEU B 350 TRP B 356 -1 N TYR B 351 O LEU B 372
SHEET 3 E 6 PHE B 314 VAL B 318 1 N TYR B 316 O SER B 354
SHEET 4 E 6 PHE B 284 VAL B 295 -1 N ALA B 292 O TYR B 317
SHEET 5 E 6 TRP B 380 GLU B 384 -1 O PHE B 383 N LEU B 286
SHEET 6 E 6 PRO B 338 PRO B 340 -1 N LEU B 339 O LEU B 382
SHEET 1 F 9 VAL B 62 ALA B 67 0
SHEET 2 F 9 GLY B 86 CYS B 89 1 O GLY B 86 N TYR B 66
SHEET 3 F 9 ILE B 108 TYR B 110 1 O ILE B 109 N PHE B 87
SHEET 4 F 9 VAL B 130 PHE B 133 1 O VAL B 130 N TYR B 110
SHEET 5 F 9 LYS B 150 ARG B 154 1 O ARG B 154 N PHE B 133
SHEET 6 F 9 VAL B 191 SER B 195 1 O GLY B 193 N LEU B 153
SHEET 7 F 9 ILE B 231 ASP B 233 1 O ASP B 233 N VAL B 194
SHEET 8 F 9 THR B 270 ALA B 273 1 O VAL B 272 N LEU B 232
SHEET 9 F 9 VAL B 62 ALA B 67 1 N THR B 63 O ILE B 271
SHEET 1 G 5 PRO C 338 PRO C 340 0
SHEET 2 G 5 TRP C 380 GLU C 384 -1 O LEU C 382 N LEU C 339
SHEET 3 G 5 PHE C 284 ALA C 292 -1 N LEU C 286 O PHE C 383
SHEET 4 G 5 PHE C 40 ASP C 44 -1 N PHE C 40 O ALA C 287
SHEET 5 G 5 THR C 404 VAL C 408 1 O TYR C 406 N ALA C 43
SHEET 1 H 6 PRO C 338 PRO C 340 0
SHEET 2 H 6 TRP C 380 GLU C 384 -1 O LEU C 382 N LEU C 339
SHEET 3 H 6 PHE C 284 ALA C 292 -1 N LEU C 286 O PHE C 383
SHEET 4 H 6 TYR C 316 VAL C 318 -1 O TYR C 317 N ALA C 292
SHEET 5 H 6 LEU C 350 TRP C 356 1 O SER C 354 N TYR C 316
SHEET 6 H 6 GLN C 365 PRO C 373 -1 O LEU C 372 N TYR C 351
SHEET 1 I 9 VAL C 62 ALA C 67 0
SHEET 2 I 9 GLY C 86 CYS C 89 1 O GLY C 86 N TYR C 66
SHEET 3 I 9 ILE C 108 TYR C 110 1 O ILE C 109 N PHE C 87
SHEET 4 I 9 VAL C 130 PHE C 133 1 O VAL C 130 N TYR C 110
SHEET 5 I 9 LYS C 150 ARG C 154 1 O VAL C 152 N MET C 131
SHEET 6 I 9 VAL C 191 SER C 195 1 O GLY C 193 N LEU C 153
SHEET 7 I 9 ILE C 231 ASP C 233 1 O ASP C 233 N VAL C 194
SHEET 8 I 9 THR C 270 ALA C 273 1 O VAL C 272 N LEU C 232
SHEET 9 I 9 VAL C 62 ALA C 67 1 N THR C 63 O ILE C 271
SHEET 1 J 6 GLN D 365 PRO D 373 0
SHEET 2 J 6 LEU D 350 TRP D 356 -1 N TYR D 351 O LEU D 372
SHEET 3 J 6 SER D 313 VAL D 318 1 N TYR D 316 O SER D 354
SHEET 4 J 6 PHE D 284 THR D 296 -1 N THR D 296 O SER D 313
SHEET 5 J 6 PHE D 40 ASP D 44 -1 N PHE D 40 O ALA D 287
SHEET 6 J 6 THR D 404 VAL D 408 1 O TYR D 406 N PHE D 41
SHEET 1 K 6 GLN D 365 PRO D 373 0
SHEET 2 K 6 LEU D 350 TRP D 356 -1 N TYR D 351 O LEU D 372
SHEET 3 K 6 SER D 313 VAL D 318 1 N TYR D 316 O SER D 354
SHEET 4 K 6 PHE D 284 THR D 296 -1 N THR D 296 O SER D 313
SHEET 5 K 6 TRP D 380 GLU D 384 -1 O PHE D 383 N LEU D 286
SHEET 6 K 6 PRO D 338 PRO D 340 -1 N LEU D 339 O LEU D 382
SHEET 1 L 9 VAL D 62 ALA D 67 0
SHEET 2 L 9 GLY D 86 CYS D 89 1 O GLY D 86 N TYR D 66
SHEET 3 L 9 ILE D 108 TYR D 110 1 O ILE D 109 N PHE D 87
SHEET 4 L 9 VAL D 130 PHE D 133 1 O VAL D 130 N TYR D 110
SHEET 5 L 9 LYS D 150 ARG D 154 1 O VAL D 152 N MET D 131
SHEET 6 L 9 VAL D 191 SER D 195 1 O GLY D 193 N LEU D 153
SHEET 7 L 9 ILE D 231 ASP D 233 1 O ASP D 233 N VAL D 194
SHEET 8 L 9 THR D 270 ALA D 273 1 O VAL D 272 N LEU D 232
SHEET 9 L 9 VAL D 62 ALA D 67 1 N THR D 63 O ILE D 271
SITE 1 AC1 8 ARG A 22 ASP A 243 LEU A 339 PRO A 340
SITE 2 AC1 8 GLN A 341 LEU A 382 GLU A 384 ASP A 385
SITE 1 AC2 12 ARG B 22 CYS B 26 ASP B 243 PRO B 340
SITE 2 AC2 12 GLN B 341 ARG B 342 GLU B 343 LEU B 382
SITE 3 AC2 12 GLU B 384 ASP B 385 HOH B 629 HOH B 631
SITE 1 AC3 8 ARG C 22 ASP C 243 PRO C 340 GLN C 341
SITE 2 AC3 8 GLU C 343 LEU C 382 GLU C 384 ASP C 385
SITE 1 AC4 17 LYS A 69 ASP A 88 HIS A 197 GLY A 236
SITE 2 AC4 17 GLY A 237 GLU A 274 GLY A 276 ARG A 277
SITE 3 AC4 17 TYR A 331 ASP A 332 TYR A 389 HOH A 610
SITE 4 AC4 17 HOH A 632 TYR B 323 CYS B 360 ASP B 361
SITE 5 AC4 17 GLY B 362
SITE 1 AC5 16 TYR A 323 CYS A 360 ASP A 361 LYS B 69
SITE 2 AC5 16 ASP B 88 ARG B 154 HIS B 197 GLY B 236
SITE 3 AC5 16 GLY B 237 GLU B 274 GLY B 276 ARG B 277
SITE 4 AC5 16 TYR B 331 ASP B 332 TYR B 389 HOH B 604
SITE 1 AC6 18 LYS C 69 ASP C 88 ARG C 154 HIS C 197
SITE 2 AC6 18 GLY C 236 GLY C 237 GLU C 274 GLY C 276
SITE 3 AC6 18 ARG C 277 TYR C 331 ASP C 332 TYR C 389
SITE 4 AC6 18 HOH C 634 HOH C 652 TYR D 323 CYS D 360
SITE 5 AC6 18 ASP D 361 HOH D 467
SITE 1 AC7 17 CYS C 360 ASP C 361 GLY C 362 LYS D 69
SITE 2 AC7 17 ASP D 88 HIS D 197 GLY D 237 GLU D 274
SITE 3 AC7 17 PRO D 275 GLY D 276 ARG D 277 TYR D 331
SITE 4 AC7 17 ASP D 332 TYR D 389 HOH D 434 HOH D 438
SITE 5 AC7 17 HOH D 442
CRYST1 67.818 88.540 150.445 90.00 90.03 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014745 0.000000 0.000008 0.00000
SCALE2 0.000000 0.011294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006647 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
