HEADER OXIDOREDUCTASE 26-MAR-08 3CNT
TITLE CRYSTAL STRUCTURE OF FMS1 IN COMPLEX WITH R-BZ-MESPERMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FMS1;
COMPND 3 CHAIN: B, A;
COMPND 4 EC: 1.5.3.11;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: FMS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS FMS1, POLYAMINE OXIDASE, N1-BENZOYL-1-METHYLSPERMIDINE, COMPLEX,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HUANG,Q.HAO
REVDAT 3 30-AUG-23 3CNT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 3CNT 1 VERSN
REVDAT 1 22-APR-08 3CNT 0
JRNL AUTH Q.HUANG,Q.HAO
JRNL TITL CRYSTAL STRUCTURE OF FMS1 IN COMPLEX WITH R-BZ-MESPERMIDINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 31701
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200
REMARK 3 FREE R VALUE TEST SET COUNT : 3170
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 453
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7723
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 125
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.06800
REMARK 3 B22 (A**2) : -4.56300
REMARK 3 B33 (A**2) : 3.49500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -21.84200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.55
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.342
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : 40.68
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 3 : FADTMP.PARAM
REMARK 3 PARAMETER FILE 4 : SUB7R.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9779
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40569
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 93.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : 0.64200
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1YY5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 0.2M LI2SO4, 0.1M TRIS
REMARK 280 -HCL, PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.92900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.20650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.92900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.20650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 VAL B 4
REMARK 465 SER B 5
REMARK 465 PRO B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 135
REMARK 465 VAL B 136
REMARK 465 SER B 137
REMARK 465 ASP B 138
REMARK 465 ASP B 344
REMARK 465 SER B 345
REMARK 465 GLN B 346
REMARK 465 LYS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 512
REMARK 465 HIS B 513
REMARK 465 HIS B 514
REMARK 465 HIS B 515
REMARK 465 HIS B 516
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 VAL A 4
REMARK 465 ASP A 344
REMARK 465 SER A 345
REMARK 465 GLN A 346
REMARK 465 LYS A 347
REMARK 465 HIS A 348
REMARK 465 PRO A 420
REMARK 465 ILE A 421
REMARK 465 GLU A 422
REMARK 465 ASN A 423
REMARK 465 ILE A 424
REMARK 465 ALA A 425
REMARK 465 ASN A 426
REMARK 465 HIS A 514
REMARK 465 HIS A 515
REMARK 465 HIS A 516
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 ARG B 87 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 GLU B 112 CG CD OE1 OE2
REMARK 470 GLN B 132 CB CG CD OE1 NE2
REMARK 470 LEU B 134 CB CG CD1 CD2
REMARK 470 LYS B 185 CG CD CE NZ
REMARK 470 ASN B 200 CB CG OD1 ND2
REMARK 470 GLN B 206 CG CD OE1 NE2
REMARK 470 GLN B 214 CG CD OE1 NE2
REMARK 470 LYS B 218 CG CD CE NZ
REMARK 470 ARG B 228 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 229 CB CG CD OE1 OE2
REMARK 470 SER B 231 OG
REMARK 470 LYS B 232 CB CG CD CE NZ
REMARK 470 ASN B 233 CG OD1 ND2
REMARK 470 GLN B 263 CB CG CD OE1 NE2
REMARK 470 PRO B 264 CB CG CD
REMARK 470 GLU B 265 CB CG CD OE1 OE2
REMARK 470 LYS B 266 CB CG CD CE NZ
REMARK 470 ALA B 285 CB
REMARK 470 LYS B 288 CG CD CE NZ
REMARK 470 ILE B 289 CB CG1 CG2 CD1
REMARK 470 HIS B 290 CB CG ND1 CD2 CE1 NE2
REMARK 470 PHE B 291 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 331 CG CD OE1 OE2
REMARK 470 LEU B 333 CG CD1 CD2
REMARK 470 ASP B 337 CB CG OD1 OD2
REMARK 470 GLU B 341 CB CG CD OE1 OE2
REMARK 470 ARG B 342 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 343 CB CG CD OE1 OE2
REMARK 470 THR B 349 OG1 CG2
REMARK 470 SER B 350 OG
REMARK 470 ILE B 424 CB CG1 CG2 CD1
REMARK 470 ALA B 427 CB
REMARK 470 ASN B 428 CG OD1 ND2
REMARK 470 ALA B 449 CB
REMARK 470 VAL B 460 CG1 CG2
REMARK 470 ASN B 468 CG OD1 ND2
REMARK 470 SER B 472 CB OG
REMARK 470 HIS B 511 CB CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 112 CG CD OE1 OE2
REMARK 470 ASN A 120 CG OD1 ND2
REMARK 470 HIS A 131 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 132 CB CG CD OE1 NE2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 ASN A 200 CB CG OD1 ND2
REMARK 470 LYS A 232 CB CG CD CE NZ
REMARK 470 LYS A 266 CG CD CE NZ
REMARK 470 ALA A 330 CB
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 LEU A 333 CG CD1 CD2
REMARK 470 ASP A 337 CG OD1 OD2
REMARK 470 SER A 338 CB OG
REMARK 470 GLU A 341 CG CD OE1 OE2
REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 343 CG CD OE1 OE2
REMARK 470 ALA A 427 CB
REMARK 470 ASN A 428 CB CG OD1 ND2
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 ASP A 458 CB CG OD1 OD2
REMARK 470 GLU A 510 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 269 NH2 ARG A 269 2555 1.98
REMARK 500 NE ARG A 269 NE ARG A 269 2555 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 PRO B 420 C - N - CA ANGL. DEV. = 11.1 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 ASP B 34 72.70 41.76
REMARK 500 VAL B 44 -146.79 -90.63
REMARK 500 GLN B 55 28.98 34.77
REMARK 500 SER B 64 -20.09 -155.95
REMARK 500 THR B 69 12.07 -62.55
REMARK 500 ASN B 72 101.47 -59.80
REMARK 500 ASN B 84 -73.89 -59.83
REMARK 500 VAL B 107 10.10 -140.63
REMARK 500 GLN B 132 74.18 51.38
REMARK 500 PHE B 189 -178.86 -68.70
REMARK 500 ASN B 200 103.53 86.75
REMARK 500 ASN B 215 15.91 -68.66
REMARK 500 SER B 220 41.44 70.31
REMARK 500 SER B 225 130.20 -173.56
REMARK 500 SER B 231 58.35 -65.41
REMARK 500 LYS B 232 27.12 39.03
REMARK 500 GLU B 239 -66.38 -23.17
REMARK 500 THR B 242 107.54 -21.25
REMARK 500 LYS B 266 71.45 -57.14
REMARK 500 ASN B 267 -34.80 -145.24
REMARK 500 LEU B 268 121.66 -21.72
REMARK 500 ARG B 269 140.71 -36.30
REMARK 500 PRO B 277 174.75 -56.69
REMARK 500 PHE B 286 27.25 -76.50
REMARK 500 ILE B 289 -164.44 28.37
REMARK 500 HIS B 290 16.72 139.05
REMARK 500 GLU B 302 -71.16 -56.28
REMARK 500 CYS B 305 67.15 -161.72
REMARK 500 ASN B 308 31.92 -98.77
REMARK 500 GLU B 341 135.06 141.58
REMARK 500 ARG B 342 -135.56 179.59
REMARK 500 SER B 350 110.27 86.67
REMARK 500 CYS B 353 -9.64 -58.73
REMARK 500 LEU B 363 -5.19 -58.98
REMARK 500 ALA B 370 68.87 -65.42
REMARK 500 SER B 411 -159.79 -148.10
REMARK 500 PRO B 420 148.25 -35.15
REMARK 500 ILE B 421 78.98 -154.48
REMARK 500 GLU B 422 117.76 -36.96
REMARK 500 ALA B 425 -19.16 -46.03
REMARK 500 ASN B 426 41.07 -83.44
REMARK 500 ALA B 427 -83.66 -55.10
REMARK 500 LYS B 429 138.24 -34.61
REMARK 500 ARG B 433 -63.95 -101.51
REMARK 500 SER B 446 -66.03 -134.62
REMARK 500 PRO B 455 95.50 -51.25
REMARK 500 VAL B 460 -59.64 -155.49
REMARK 500 ASP B 471 -157.28 -154.33
REMARK 500 ALA B 486 134.36 -39.30
REMARK 500 ALA A 7 126.21 -38.41
REMARK 500
REMARK 500 THIS ENTRY HAS 89 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 FAD A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SP9 B 518
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YY5 RELATED DB: PDB
REMARK 900 NATIVE FMS1
REMARK 900 RELATED ID: 1XPQ RELATED DB: PDB
REMARK 900 FMS1 IN COMPLEX WITH ITS NATIVE SUBSTRATE SPERMINE
REMARK 900 RELATED ID: 3CN8 RELATED DB: PDB
REMARK 900 FMS1 IN COMPLEX WITH SPERMIDINE
REMARK 900 RELATED ID: 3CND RELATED DB: PDB
REMARK 900 FMS1 IN COMPLEX WITH N1-ACSPERMINE
REMARK 900 RELATED ID: 3CNP RELATED DB: PDB
REMARK 900 FMS1 IN COMPLEX WITH S-N1-ACMESPERMIDINE
REMARK 900 RELATED ID: 3CNS RELATED DB: PDB
REMARK 900 FMS1 IN COMPLEX WITH S-BZ-MESPERMIDINE
DBREF 3CNT A 1 508 UNP P50264 FMS1_YEAST 1 508
DBREF 3CNT B 1 508 UNP P50264 FMS1_YEAST 1 508
SEQADV 3CNT LEU B 509 UNP P50264 EXPRESSION TAG
SEQADV 3CNT GLU B 510 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 511 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 512 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 513 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 514 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 515 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS B 516 UNP P50264 EXPRESSION TAG
SEQADV 3CNT LEU A 509 UNP P50264 EXPRESSION TAG
SEQADV 3CNT GLU A 510 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 511 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 512 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 513 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 514 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 515 UNP P50264 EXPRESSION TAG
SEQADV 3CNT HIS A 516 UNP P50264 EXPRESSION TAG
SEQRES 1 B 516 MET ASN THR VAL SER PRO ALA LYS LYS LYS VAL ILE ILE
SEQRES 2 B 516 ILE GLY ALA GLY ILE ALA GLY LEU LYS ALA ALA SER THR
SEQRES 3 B 516 LEU HIS GLN ASN GLY ILE GLN ASP CYS LEU VAL LEU GLU
SEQRES 4 B 516 ALA ARG ASP ARG VAL GLY GLY ARG LEU GLN THR VAL THR
SEQRES 5 B 516 GLY TYR GLN GLY ARG LYS TYR ASP ILE GLY ALA SER TRP
SEQRES 6 B 516 HIS HIS ASP THR LEU THR ASN PRO LEU PHE LEU GLU GLU
SEQRES 7 B 516 ALA GLN LEU SER LEU ASN ASP GLY ARG THR ARG PHE VAL
SEQRES 8 B 516 PHE ASP ASP ASP ASN PHE ILE TYR ILE ASP GLU GLU ARG
SEQRES 9 B 516 GLY ARG VAL ASP HIS ASP LYS GLU LEU LEU LEU GLU ILE
SEQRES 10 B 516 VAL ASP ASN GLU MET SER LYS PHE ALA GLU LEU GLU PHE
SEQRES 11 B 516 HIS GLN HIS LEU GLY VAL SER ASP CYS SER PHE PHE GLN
SEQRES 12 B 516 LEU VAL MET LYS TYR LEU LEU GLN ARG ARG GLN PHE LEU
SEQRES 13 B 516 THR ASN ASP GLN ILE ARG TYR LEU PRO GLN LEU CYS ARG
SEQRES 14 B 516 TYR LEU GLU LEU TRP HIS GLY LEU ASP TRP LYS LEU LEU
SEQRES 15 B 516 SER ALA LYS ASP THR TYR PHE GLY HIS GLN GLY ARG ASN
SEQRES 16 B 516 ALA PHE ALA LEU ASN TYR ASP SER VAL VAL GLN ARG ILE
SEQRES 17 B 516 ALA GLN SER PHE PRO GLN ASN TRP LEU LYS LEU SER CYS
SEQRES 18 B 516 GLU VAL LYS SER ILE THR ARG GLU PRO SER LYS ASN VAL
SEQRES 19 B 516 THR VAL ASN CYS GLU ASP GLY THR VAL TYR ASN ALA ASP
SEQRES 20 B 516 TYR VAL ILE ILE THR VAL PRO GLN SER VAL LEU ASN LEU
SEQRES 21 B 516 SER VAL GLN PRO GLU LYS ASN LEU ARG GLY ARG ILE GLU
SEQRES 22 B 516 PHE GLN PRO PRO LEU LYS PRO VAL ILE GLN ASP ALA PHE
SEQRES 23 B 516 ASP LYS ILE HIS PHE GLY ALA LEU GLY LYS VAL ILE PHE
SEQRES 24 B 516 GLU PHE GLU GLU CYS CYS TRP SER ASN GLU SER SER LYS
SEQRES 25 B 516 ILE VAL THR LEU ALA ASN SER THR ASN GLU PHE VAL GLU
SEQRES 26 B 516 ILE VAL ARG ASN ALA GLU ASN LEU ASP GLU LEU ASP SER
SEQRES 27 B 516 MET LEU GLU ARG GLU ASP SER GLN LYS HIS THR SER VAL
SEQRES 28 B 516 THR CYS TRP SER GLN PRO LEU PHE PHE VAL ASN LEU SER
SEQRES 29 B 516 LYS SER THR GLY VAL ALA SER PHE MET MET LEU MET GLN
SEQRES 30 B 516 ALA PRO LEU THR ASN HIS ILE GLU SER ILE ARG GLU ASP
SEQRES 31 B 516 LYS GLU ARG LEU PHE SER PHE PHE GLN PRO VAL LEU ASN
SEQRES 32 B 516 LYS ILE MET LYS CYS LEU ASP SER GLU ASP VAL ILE ASP
SEQRES 33 B 516 GLY MET ARG PRO ILE GLU ASN ILE ALA ASN ALA ASN LYS
SEQRES 34 B 516 PRO VAL LEU ARG ASN ILE ILE VAL SER ASN TRP THR ARG
SEQRES 35 B 516 ASP PRO TYR SER ARG GLY ALA TYR SER ALA CYS PHE PRO
SEQRES 36 B 516 GLY ASP ASP PRO VAL ASP MET VAL VAL ALA MET SER ASN
SEQRES 37 B 516 GLY GLN ASP SER ARG ILE ARG PHE ALA GLY GLU HIS THR
SEQRES 38 B 516 ILE MET ASP GLY ALA GLY CYS ALA TYR GLY ALA TRP GLU
SEQRES 39 B 516 SER GLY ARG ARG GLU ALA THR ARG ILE SER ASP LEU LEU
SEQRES 40 B 516 LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 A 516 MET ASN THR VAL SER PRO ALA LYS LYS LYS VAL ILE ILE
SEQRES 2 A 516 ILE GLY ALA GLY ILE ALA GLY LEU LYS ALA ALA SER THR
SEQRES 3 A 516 LEU HIS GLN ASN GLY ILE GLN ASP CYS LEU VAL LEU GLU
SEQRES 4 A 516 ALA ARG ASP ARG VAL GLY GLY ARG LEU GLN THR VAL THR
SEQRES 5 A 516 GLY TYR GLN GLY ARG LYS TYR ASP ILE GLY ALA SER TRP
SEQRES 6 A 516 HIS HIS ASP THR LEU THR ASN PRO LEU PHE LEU GLU GLU
SEQRES 7 A 516 ALA GLN LEU SER LEU ASN ASP GLY ARG THR ARG PHE VAL
SEQRES 8 A 516 PHE ASP ASP ASP ASN PHE ILE TYR ILE ASP GLU GLU ARG
SEQRES 9 A 516 GLY ARG VAL ASP HIS ASP LYS GLU LEU LEU LEU GLU ILE
SEQRES 10 A 516 VAL ASP ASN GLU MET SER LYS PHE ALA GLU LEU GLU PHE
SEQRES 11 A 516 HIS GLN HIS LEU GLY VAL SER ASP CYS SER PHE PHE GLN
SEQRES 12 A 516 LEU VAL MET LYS TYR LEU LEU GLN ARG ARG GLN PHE LEU
SEQRES 13 A 516 THR ASN ASP GLN ILE ARG TYR LEU PRO GLN LEU CYS ARG
SEQRES 14 A 516 TYR LEU GLU LEU TRP HIS GLY LEU ASP TRP LYS LEU LEU
SEQRES 15 A 516 SER ALA LYS ASP THR TYR PHE GLY HIS GLN GLY ARG ASN
SEQRES 16 A 516 ALA PHE ALA LEU ASN TYR ASP SER VAL VAL GLN ARG ILE
SEQRES 17 A 516 ALA GLN SER PHE PRO GLN ASN TRP LEU LYS LEU SER CYS
SEQRES 18 A 516 GLU VAL LYS SER ILE THR ARG GLU PRO SER LYS ASN VAL
SEQRES 19 A 516 THR VAL ASN CYS GLU ASP GLY THR VAL TYR ASN ALA ASP
SEQRES 20 A 516 TYR VAL ILE ILE THR VAL PRO GLN SER VAL LEU ASN LEU
SEQRES 21 A 516 SER VAL GLN PRO GLU LYS ASN LEU ARG GLY ARG ILE GLU
SEQRES 22 A 516 PHE GLN PRO PRO LEU LYS PRO VAL ILE GLN ASP ALA PHE
SEQRES 23 A 516 ASP LYS ILE HIS PHE GLY ALA LEU GLY LYS VAL ILE PHE
SEQRES 24 A 516 GLU PHE GLU GLU CYS CYS TRP SER ASN GLU SER SER LYS
SEQRES 25 A 516 ILE VAL THR LEU ALA ASN SER THR ASN GLU PHE VAL GLU
SEQRES 26 A 516 ILE VAL ARG ASN ALA GLU ASN LEU ASP GLU LEU ASP SER
SEQRES 27 A 516 MET LEU GLU ARG GLU ASP SER GLN LYS HIS THR SER VAL
SEQRES 28 A 516 THR CYS TRP SER GLN PRO LEU PHE PHE VAL ASN LEU SER
SEQRES 29 A 516 LYS SER THR GLY VAL ALA SER PHE MET MET LEU MET GLN
SEQRES 30 A 516 ALA PRO LEU THR ASN HIS ILE GLU SER ILE ARG GLU ASP
SEQRES 31 A 516 LYS GLU ARG LEU PHE SER PHE PHE GLN PRO VAL LEU ASN
SEQRES 32 A 516 LYS ILE MET LYS CYS LEU ASP SER GLU ASP VAL ILE ASP
SEQRES 33 A 516 GLY MET ARG PRO ILE GLU ASN ILE ALA ASN ALA ASN LYS
SEQRES 34 A 516 PRO VAL LEU ARG ASN ILE ILE VAL SER ASN TRP THR ARG
SEQRES 35 A 516 ASP PRO TYR SER ARG GLY ALA TYR SER ALA CYS PHE PRO
SEQRES 36 A 516 GLY ASP ASP PRO VAL ASP MET VAL VAL ALA MET SER ASN
SEQRES 37 A 516 GLY GLN ASP SER ARG ILE ARG PHE ALA GLY GLU HIS THR
SEQRES 38 A 516 ILE MET ASP GLY ALA GLY CYS ALA TYR GLY ALA TRP GLU
SEQRES 39 A 516 SER GLY ARG ARG GLU ALA THR ARG ILE SER ASP LEU LEU
SEQRES 40 A 516 LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET FAD B 517 53
HET SP9 B 518 19
HET FAD A 517 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SP9 N-{(1R)-3-[(4-AMINOBUTYL)AMINO]-1-
HETNAM 2 SP9 METHYLPROPYL}BENZAMIDE
HETSYN SP9 R-BZ-MESPERMIDINE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 SP9 C15 H25 N3 O
FORMUL 6 HOH *51(H2 O)
HELIX 1 1 GLY B 17 ASN B 30 1 14
HELIX 2 2 TYR B 54 GLY B 56 5 3
HELIX 3 3 ASN B 72 GLY B 86 1 15
HELIX 4 4 LEU B 114 HIS B 131 1 18
HELIX 5 5 SER B 140 ARG B 153 1 14
HELIX 6 6 GLN B 154 LEU B 156 5 3
HELIX 7 7 THR B 157 ARG B 169 1 13
HELIX 8 8 LEU B 171 GLY B 176 1 6
HELIX 9 9 SER B 183 TYR B 188 1 6
HELIX 10 10 TYR B 201 SER B 211 1 11
HELIX 11 11 PHE B 212 LEU B 217 5 6
HELIX 12 12 PRO B 254 ASN B 259 1 6
HELIX 13 13 LEU B 260 GLN B 263 5 4
HELIX 14 14 LYS B 279 PHE B 286 1 8
HELIX 15 15 THR B 320 ALA B 330 1 11
HELIX 16 16 ASP B 334 MET B 339 1 6
HELIX 17 17 LEU B 363 GLY B 368 1 6
HELIX 18 18 PRO B 379 ILE B 387 1 9
HELIX 19 19 ASP B 390 LEU B 409 1 20
HELIX 20 20 VAL B 460 SER B 467 1 8
HELIX 21 21 CYS B 488 GLU B 510 1 23
HELIX 22 22 GLY A 17 ASN A 30 1 14
HELIX 23 23 TYR A 54 GLY A 56 5 3
HELIX 24 24 ASN A 72 GLY A 86 1 15
HELIX 25 25 LEU A 114 PHE A 130 1 17
HELIX 26 26 SER A 140 ARG A 152 1 13
HELIX 27 27 ARG A 153 LEU A 156 5 4
HELIX 28 28 THR A 157 ARG A 169 1 13
HELIX 29 29 LEU A 171 GLY A 176 1 6
HELIX 30 30 SER A 183 TYR A 188 1 6
HELIX 31 31 TYR A 201 GLN A 210 1 10
HELIX 32 32 PRO A 254 LEU A 260 1 7
HELIX 33 33 SER A 261 GLN A 263 5 3
HELIX 34 34 LYS A 279 ASP A 284 1 6
HELIX 35 35 ALA A 285 ILE A 289 5 5
HELIX 36 36 THR A 320 ALA A 330 1 11
HELIX 37 37 ASN A 332 GLU A 341 1 10
HELIX 38 38 LEU A 363 THR A 367 1 5
HELIX 39 39 PRO A 379 ILE A 387 1 9
HELIX 40 40 ASP A 390 LEU A 409 1 20
HELIX 41 41 ASP A 458 GLY A 469 1 12
HELIX 42 42 CYS A 488 LEU A 509 1 22
HELIX 43 43 GLU A 510 HIS A 512 5 3
SHEET 1 A 6 CYS B 35 LEU B 38 0
SHEET 2 A 6 LYS B 9 ILE B 14 1 N ILE B 13 O LEU B 36
SHEET 3 A 6 VAL B 243 ILE B 251 1 O ILE B 250 N ILE B 14
SHEET 4 A 6 ASN B 233 CYS B 238 -1 N VAL B 234 O ALA B 246
SHEET 5 A 6 VAL B 223 GLU B 229 -1 N THR B 227 O THR B 235
SHEET 6 A 6 GLU B 273 GLN B 275 1 O GLN B 275 N ILE B 226
SHEET 1 B 4 CYS B 35 LEU B 38 0
SHEET 2 B 4 LYS B 9 ILE B 14 1 N ILE B 13 O LEU B 36
SHEET 3 B 4 VAL B 243 ILE B 251 1 O ILE B 250 N ILE B 14
SHEET 4 B 4 ILE B 474 PHE B 476 1 O ARG B 475 N ILE B 251
SHEET 1 C 2 THR B 50 THR B 52 0
SHEET 2 C 2 LYS B 58 ASP B 60 -1 O TYR B 59 N VAL B 51
SHEET 1 D 3 TRP B 65 HIS B 66 0
SHEET 2 D 3 ALA B 196 ALA B 198 -1 O ALA B 196 N HIS B 66
SHEET 3 D 3 PHE B 90 VAL B 91 -1 N VAL B 91 O PHE B 197
SHEET 1 E 8 GLY B 105 ARG B 106 0
SHEET 2 E 8 ILE B 98 ASP B 101 -1 N ASP B 101 O GLY B 105
SHEET 3 E 8 LYS B 312 LEU B 316 1 O LEU B 316 N ILE B 100
SHEET 4 E 8 LEU B 358 ASN B 362 -1 O PHE B 360 N ILE B 313
SHEET 5 E 8 SER B 371 MET B 376 -1 O MET B 373 N VAL B 361
SHEET 6 E 8 GLY B 295 PHE B 301 -1 N PHE B 299 O PHE B 372
SHEET 7 E 8 VAL B 431 VAL B 437 -1 O ARG B 433 N GLU B 300
SHEET 8 E 8 ILE B 415 ASP B 416 1 N ILE B 415 O LEU B 432
SHEET 1 F 7 LEU A 217 LYS A 218 0
SHEET 2 F 7 LEU A 36 LEU A 38 1 N VAL A 37 O LYS A 218
SHEET 3 F 7 ALA A 7 ILE A 14 1 N ILE A 13 O LEU A 36
SHEET 4 F 7 VAL A 243 ILE A 251 1 O ASN A 245 N ALA A 7
SHEET 5 F 7 ASN A 233 CYS A 238 -1 N VAL A 234 O ALA A 246
SHEET 6 F 7 VAL A 223 GLU A 229 -1 N GLU A 229 O ASN A 233
SHEET 7 F 7 GLU A 273 GLN A 275 1 O GLN A 275 N ARG A 228
SHEET 1 G 5 LEU A 217 LYS A 218 0
SHEET 2 G 5 LEU A 36 LEU A 38 1 N VAL A 37 O LYS A 218
SHEET 3 G 5 ALA A 7 ILE A 14 1 N ILE A 13 O LEU A 36
SHEET 4 G 5 VAL A 243 ILE A 251 1 O ASN A 245 N ALA A 7
SHEET 5 G 5 ILE A 474 PHE A 476 1 O ARG A 475 N VAL A 249
SHEET 1 H 2 THR A 50 THR A 52 0
SHEET 2 H 2 LYS A 58 ASP A 60 -1 O TYR A 59 N VAL A 51
SHEET 1 I 3 TRP A 65 HIS A 66 0
SHEET 2 I 3 ALA A 196 ALA A 198 -1 O ALA A 196 N HIS A 66
SHEET 3 I 3 PHE A 90 VAL A 91 -1 N VAL A 91 O PHE A 197
SHEET 1 J 8 GLY A 105 ARG A 106 0
SHEET 2 J 8 ILE A 98 ASP A 101 -1 N ASP A 101 O GLY A 105
SHEET 3 J 8 LYS A 312 THR A 315 1 O VAL A 314 N ILE A 98
SHEET 4 J 8 LEU A 358 ASN A 362 -1 O PHE A 360 N ILE A 313
SHEET 5 J 8 SER A 371 MET A 376 -1 O LEU A 375 N PHE A 359
SHEET 6 J 8 GLY A 295 PHE A 301 -1 N PHE A 299 O PHE A 372
SHEET 7 J 8 VAL A 431 VAL A 437 -1 O ILE A 436 N ILE A 298
SHEET 8 J 8 ILE A 415 ASP A 416 1 N ILE A 415 O LEU A 432
SHEET 1 K 2 HIS A 290 GLY A 292 0
SHEET 2 K 2 TYR A 450 ALA A 452 -1 O TYR A 450 N GLY A 292
SSBOND 1 CYS B 221 CYS B 238 1555 1555 2.03
SSBOND 2 CYS A 221 CYS A 238 1555 1555 2.04
CISPEP 1 GLN B 275 PRO B 276 0 0.00
CISPEP 2 ALA B 378 PRO B 379 0 0.30
CISPEP 3 GLN A 275 PRO A 276 0 -0.42
CISPEP 4 ALA A 378 PRO A 379 0 0.42
SITE 1 AC1 30 GLY A 15 GLY A 17 ILE A 18 ALA A 19
SITE 2 AC1 30 GLU A 39 ALA A 40 ARG A 41 GLY A 45
SITE 3 AC1 30 GLY A 46 ARG A 47 GLY A 62 ALA A 63
SITE 4 AC1 30 SER A 64 TRP A 65 HIS A 67 CYS A 221
SITE 5 AC1 30 GLU A 222 THR A 252 PRO A 254 GLY A 270
SITE 6 AC1 30 LEU A 294 TRP A 440 ALA A 449 TYR A 450
SITE 7 AC1 30 GLY A 478 GLU A 479 GLY A 487 CYS A 488
SITE 8 AC1 30 ALA A 489 ALA A 492
SITE 1 AC2 30 GLY B 15 GLY B 17 ILE B 18 ALA B 19
SITE 2 AC2 30 LEU B 38 GLU B 39 ALA B 40 ARG B 41
SITE 3 AC2 30 GLY B 46 ARG B 47 LEU B 48 GLY B 62
SITE 4 AC2 30 ALA B 63 SER B 64 TRP B 65 HIS B 67
SITE 5 AC2 30 CYS B 221 THR B 252 GLY B 270 LEU B 294
SITE 6 AC2 30 TRP B 440 TYR B 445 ALA B 449 TYR B 450
SITE 7 AC2 30 GLY B 478 GLU B 479 GLY B 487 CYS B 488
SITE 8 AC2 30 ALA B 489 ALA B 492
SITE 1 AC3 9 TRP B 65 HIS B 67 LEU B 173 TRP B 174
SITE 2 AC3 9 PHE B 359 LEU B 375 TYR B 450 ALA B 486
SITE 3 AC3 9 CYS B 488
CRYST1 161.858 102.413 77.204 90.00 94.94 90.00 C 1 2 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 0.006178 0.000000 0.000534 0.00000
SCALE2 0.000000 0.009764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END