HEADER OXIDOREDUCTASE 24-JAN-01 1H81
TITLE STRUCTURE OF POLYAMINE OXIDASE IN THE REDUCED STATE
CAVEAT 1H81 THR C 386 HAS WRONG CHIRALITY AT ATOM CB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYAMINE OXIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: FAD-BINDING DOMAIN RESIDUES 29-500;
COMPND 5 EC: 1.5.3.11
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577
KEYWDS FLAVIN-DEPENDENT AMINE OXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BINDA,A.CODA,R.ANGELINI,R.FEDERICO,P.ASCENZI,A.MATTEVI
REVDAT 6 13-DEC-23 1H81 1 REMARK HETSYN LINK
REVDAT 5 29-JUL-20 1H81 1 CAVEAT COMPND REMARK HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 24-JUL-19 1H81 1 REMARK LINK
REVDAT 3 24-FEB-09 1H81 1 VERSN
REVDAT 2 27-MAR-01 1H81 1 JRNL
REVDAT 1 31-JAN-01 1H81 0
JRNL AUTH C.BINDA,R.ANGELINI,R.FEDERICO,P.ASCENZI,A.MATTEVI
JRNL TITL STRUCTURAL BASES FOR INHIBITOR BINDING AND CATALYSIS IN
JRNL TITL 2 POLYAMINE OXIDASE
JRNL REF BIOCHEMISTRY V. 40 2766 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11258887
JRNL DOI 10.1021/BI002751J
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5D
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 156392
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1910
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1910
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 2.00
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 156392
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 275
REMARK 3 SOLVENT ATOMS : 724
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.009 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.200 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.013 ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.015 ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT PROTGEO
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1290005824.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 156868
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : NULL
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: CCP4
REMARK 200 STARTING MODEL: 1B37
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 185.02000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.51000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 138.76500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.25500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 231.27500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 185.02000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 92.51000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 46.25500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 138.76500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 231.27500
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 300 REMARK: IN THE CRYSTAL WHILE THE CHAIN C FORMS A
REMARK 300 HOMODIMERWITH A SYMMETRY RELATED MOLECULE. THE
REMARK 300 PROTEIN ISACTIVE AS A MONOMER.
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 90.88500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 157.41744
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.25500
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYSES THE OXIDATION OF THE SECONDARY AMINO GROUP OF
REMARK 400 POLYAMINES (SPERMINE, SPERMIDINE AND THEIR ACETYL DERIVATIVES)
REMARK 400 THIS IS IMPORTANT FOR REGULATION OF POLYAMINE INTRACELLULAR
REMARK 400 CONCENTRATION.
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 ALA A 1
REMARK 465 THR A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 4
REMARK 465 LYS A 464
REMARK 465 TYR A 465
REMARK 465 HIS A 466
REMARK 465 VAL A 467
REMARK 465 GLN A 468
REMARK 465 GLY A 469
REMARK 465 LYS A 470
REMARK 465 TYR A 471
REMARK 465 ASP A 472
REMARK 465 ALA B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 GLY B 4
REMARK 465 VAL B 467
REMARK 465 GLN B 468
REMARK 465 GLY B 469
REMARK 465 LYS B 470
REMARK 465 TYR B 471
REMARK 465 ASP B 472
REMARK 465 ALA C 1
REMARK 465 THR C 2
REMARK 465 VAL C 3
REMARK 465 GLY C 4
REMARK 465 VAL C 467
REMARK 465 GLN C 468
REMARK 465 GLY C 469
REMARK 465 LYS C 470
REMARK 465 TYR C 471
REMARK 465 ASP C 472
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 LYS A 68 CD CE NZ
REMARK 480 LYS A 81 CE NZ
REMARK 480 LYS A 98 CE NZ
REMARK 480 LYS A 111 CG CD CE NZ
REMARK 480 LYS A 125 CD CE NZ
REMARK 480 ARG A 135 CZ NH1 NH2
REMARK 480 LYS A 218 CD CE NZ
REMARK 480 ASP A 221 CG OD1 OD2
REMARK 480 LYS A 222 CG CD CE NZ
REMARK 480 LYS A 225 CG CD CE NZ
REMARK 480 LYS A 279 CD CE NZ
REMARK 480 LYS A 308 CD CE NZ
REMARK 480 LYS A 314 CG CD CE NZ
REMARK 480 GLU A 363 CG CD OE1 OE2
REMARK 480 GLN A 364 CG CD OE1 NE2
REMARK 480 LYS A 380 CD CE NZ
REMARK 480 ASP A 381 CG OD1 OD2
REMARK 480 LYS B 68 CD CE NZ
REMARK 480 LYS B 81 CB CG CD CE NZ
REMARK 480 LYS B 111 CE NZ
REMARK 480 GLU B 121 CG CD OE1 OE2
REMARK 480 GLN B 202 CG CD OE1 NE2
REMARK 480 LYS B 218 CD CE NZ
REMARK 480 LYS B 222 CB CG CD CE NZ
REMARK 480 LYS B 225 CE NZ
REMARK 480 LYS B 241 CE NZ
REMARK 480 LYS B 279 CD CE NZ
REMARK 480 LYS B 281 CD CE NZ
REMARK 480 LYS B 314 CG CD CE NZ
REMARK 480 GLU B 363 CD OE1 OE2
REMARK 480 GLN B 364 CD OE1 NE2
REMARK 480 LYS B 380 CD CE NZ
REMARK 480 GLU B 434 OE1 OE2
REMARK 480 LYS B 460 CD CE NZ
REMARK 480 LYS B 461 CE NZ
REMARK 480 LYS B 464 CB CG CD CE NZ
REMARK 480 LYS C 81 CE NZ
REMARK 480 LYS C 111 CE NZ
REMARK 480 ARG C 135 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 218 CG CD CE NZ
REMARK 480 ASP C 221 CG OD1 OD2
REMARK 480 LYS C 222 CB CG CD CE NZ
REMARK 480 LYS C 225 CG CD CE NZ
REMARK 480 LYS C 250 CE NZ
REMARK 480 ASP C 274 CB CG OD1 OD2
REMARK 480 LYS C 314 CD CE NZ
REMARK 480 GLU C 363 CG CD OE1 OE2
REMARK 480 GLN C 364 CD OE1 NE2
REMARK 480 LYS C 380 CE NZ
REMARK 480 GLU C 414 CD OE1 OE2
REMARK 480 LYS C 464 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2015 O HOH A 2050 1.82
REMARK 500 O4 NAG F 2 O5 MAN F 3 1.88
REMARK 500 O HOH A 2016 O HOH A 2052 1.91
REMARK 500 O HOH A 2003 O HOH A 2009 2.07
REMARK 500 OE1 GLN C 292 O HOH C 2137 2.07
REMARK 500 O HOH C 2013 O HOH C 2082 2.07
REMARK 500 ND2 ASN B 77 O5 NAG E 1 2.10
REMARK 500 OD1 ASP A 117 O HOH A 2050 2.11
REMARK 500 ND2 ASN A 77 O5 NAG D 1 2.13
REMARK 500 O HOH B 2221 O HOH B 2225 2.16
REMARK 500 ND2 ASN C 77 O5 NAG F 1 2.16
REMARK 500 O HOH C 2106 O HOH C 2108 2.17
REMARK 500 O3 NAG F 1 C2 FCA F 5 2.17
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 VAL A 61 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 GLY A 101 N - CA - C ANGL. DEV. = 17.9 DEGREES
REMARK 500 ASP A 117 CB - CG - OD1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 136 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 260 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 326 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 351 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG A 355 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 355 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 VAL B 61 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 ARG B 135 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 GLU B 252 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASP B 351 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 355 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 6 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP C 105 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 112 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 LEU C 115 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG C 145 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 145 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG C 176 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 230 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG C 307 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG C 355 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG C 397 NE - CZ - NH2 ANGL. DEV. = -3.0 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 ALA A 12 40.21 -107.94
REMARK 500 SER A 78 -62.75 -109.47
REMARK 500 PHE A 167 -62.01 -124.78
REMARK 500 THR A 183 -17.44 -142.36
REMARK 500 TYR A 216 -9.99 -153.36
REMARK 500 LYS A 222 -63.66 -97.49
REMARK 500 ASN A 254 4.79 83.80
REMARK 500 TYR A 329 51.05 34.40
REMARK 500 PHE A 335 43.33 -107.33
REMARK 500 ASP A 341 -1.33 74.67
REMARK 500 ASP A 351 -120.90 47.70
REMARK 500 PHE A 377 59.66 -114.56
REMARK 500 ARG A 392 56.30 -113.75
REMARK 500 TYR A 399 -46.96 -139.62
REMARK 500 SER B 78 -56.45 -132.14
REMARK 500 ASP B 100 40.87 -106.97
REMARK 500 TYR B 216 -5.63 -147.98
REMARK 500 TYR B 329 54.91 38.42
REMARK 500 ASP B 351 -121.74 45.32
REMARK 500 ARG B 392 62.04 -117.19
REMARK 500 TYR B 399 -48.19 -136.02
REMARK 500 ASN C 59 -18.68 -140.39
REMARK 500 SER C 78 -51.83 -127.27
REMARK 500 TYR C 216 -14.10 -143.34
REMARK 500 LYS C 222 -76.22 -88.14
REMARK 500 ASN C 254 -2.71 82.51
REMARK 500 ASP C 351 -125.46 45.30
REMARK 500 TYR C 399 -45.61 -135.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B37 RELATED DB: PDB
REMARK 900 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF
REMARK 900 POLYAMINE OXIDASE
REMARK 900 RELATED ID: 1B5Q RELATED DB: PDB
REMARK 900 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF
REMARK 900 POLYAMINE OXIDASE
REMARK 900 RELATED ID: 1H82 RELATED DB: PDB
REMARK 900 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH GUAZATINE
REMARK 900 RELATED ID: 1H83 RELATED DB: PDB
REMARK 900 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE
REMARK 900 RELATED ID: 1H84 RELATED DB: PDB
REMARK 900 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND
REMARK 900 N1ETHYLN11((CYCLOHEPTYL)METHYL)4, 8DIAZAUNDECANE AT PH 4.6
REMARK 900 RELATED ID: 1H86 RELATED DB: PDB
REMARK 900 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND
REMARK 900 N1ETHYLN11((CYCLOHEPTYL)METHYL)4, 8DIAZAUNDECANE AT PH 7.0
DBREF 1H81 A 1 472 UNP O64411 PAO_MAIZE 29 500
DBREF 1H81 B 1 472 UNP O64411 PAO_MAIZE 29 500
DBREF 1H81 C 1 472 UNP O64411 PAO_MAIZE 29 500
SEQRES 1 A 472 ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY
SEQRES 2 A 472 MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA
SEQRES 3 A 472 GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS
SEQRES 4 A 472 ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE
SEQRES 5 A 472 ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN
SEQRES 6 A 472 GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER
SEQRES 7 A 472 THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR
SEQRES 8 A 472 LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR
SEQRES 9 A 472 ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP
SEQRES 10 A 472 SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU
SEQRES 11 A 472 HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET
SEQRES 12 A 472 GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR
SEQRES 13 A 472 PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR
SEQRES 14 A 472 GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN
SEQRES 15 A 472 THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP
SEQRES 16 A 472 VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL
SEQRES 17 A 472 VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP
SEQRES 18 A 472 LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN
SEQRES 19 A 472 LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL
SEQRES 20 A 472 THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP
SEQRES 21 A 472 TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER
SEQRES 22 A 472 ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS
SEQRES 23 A 472 VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR
SEQRES 24 A 472 LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU
SEQRES 25 A 472 GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG
SEQRES 26 A 472 ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN
SEQRES 27 A 472 TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP
SEQRES 28 A 472 GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN
SEQRES 29 A 472 THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE
SEQRES 30 A 472 PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL
SEQRES 31 A 472 PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE
SEQRES 32 A 472 SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP
SEQRES 33 A 472 GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY
SEQRES 34 A 472 GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY
SEQRES 35 A 472 ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE
SEQRES 36 A 472 ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN
SEQRES 37 A 472 GLY LYS TYR ASP
SEQRES 1 B 472 ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY
SEQRES 2 B 472 MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA
SEQRES 3 B 472 GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS
SEQRES 4 B 472 ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE
SEQRES 5 B 472 ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN
SEQRES 6 B 472 GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER
SEQRES 7 B 472 THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR
SEQRES 8 B 472 LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR
SEQRES 9 B 472 ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP
SEQRES 10 B 472 SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU
SEQRES 11 B 472 HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET
SEQRES 12 B 472 GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR
SEQRES 13 B 472 PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR
SEQRES 14 B 472 GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN
SEQRES 15 B 472 THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP
SEQRES 16 B 472 VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL
SEQRES 17 B 472 VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP
SEQRES 18 B 472 LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN
SEQRES 19 B 472 LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL
SEQRES 20 B 472 THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP
SEQRES 21 B 472 TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER
SEQRES 22 B 472 ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS
SEQRES 23 B 472 VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR
SEQRES 24 B 472 LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU
SEQRES 25 B 472 GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG
SEQRES 26 B 472 ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN
SEQRES 27 B 472 TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP
SEQRES 28 B 472 GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN
SEQRES 29 B 472 THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE
SEQRES 30 B 472 PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL
SEQRES 31 B 472 PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE
SEQRES 32 B 472 SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP
SEQRES 33 B 472 GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY
SEQRES 34 B 472 GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY
SEQRES 35 B 472 ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE
SEQRES 36 B 472 ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN
SEQRES 37 B 472 GLY LYS TYR ASP
SEQRES 1 C 472 ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY
SEQRES 2 C 472 MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA
SEQRES 3 C 472 GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS
SEQRES 4 C 472 ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE
SEQRES 5 C 472 ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN
SEQRES 6 C 472 GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER
SEQRES 7 C 472 THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR
SEQRES 8 C 472 LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR
SEQRES 9 C 472 ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP
SEQRES 10 C 472 SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU
SEQRES 11 C 472 HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET
SEQRES 12 C 472 GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR
SEQRES 13 C 472 PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR
SEQRES 14 C 472 GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN
SEQRES 15 C 472 THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP
SEQRES 16 C 472 VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL
SEQRES 17 C 472 VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP
SEQRES 18 C 472 LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN
SEQRES 19 C 472 LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL
SEQRES 20 C 472 THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP
SEQRES 21 C 472 TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER
SEQRES 22 C 472 ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS
SEQRES 23 C 472 VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR
SEQRES 24 C 472 LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU
SEQRES 25 C 472 GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG
SEQRES 26 C 472 ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN
SEQRES 27 C 472 TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP
SEQRES 28 C 472 GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN
SEQRES 29 C 472 THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE
SEQRES 30 C 472 PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL
SEQRES 31 C 472 PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE
SEQRES 32 C 472 SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP
SEQRES 33 C 472 GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY
SEQRES 34 C 472 GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY
SEQRES 35 C 472 ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE
SEQRES 36 C 472 ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN
SEQRES 37 C 472 GLY LYS TYR ASP
MODRES 1H81 ASN A 77 ASN GLYCOSYLATION SITE
MODRES 1H81 ASN B 77 ASN GLYCOSYLATION SITE
MODRES 1H81 ASN C 77 ASN GLYCOSYLATION SITE
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET MAN F 3 11
HET MAN F 4 11
HET FCA F 5 10
HET FAD A 579 53
HET FAD B 579 53
HET FAD C 579 53
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FCA ALPHA-D-FUCOPYRANOSE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FCA ALPHA-D-FUCOSE; 6-DEOXY-ALPHA-D-GALACTOPYRANOSE; D-
HETSYN 2 FCA FUCOSE; FUCOSE
FORMUL 4 NAG 6(C8 H15 N O6)
FORMUL 6 MAN 2(C6 H12 O6)
FORMUL 6 FCA C6 H12 O5
FORMUL 7 FAD 3(C27 H33 N9 O15 P2)
FORMUL 10 HOH *724(H2 O)
HELIX 1 1 GLY A 13 ALA A 26 1 14
HELIX 2 2 PRO A 71 SER A 78 1 8
HELIX 3 3 TYR A 91 GLN A 94 5 4
HELIX 4 4 ASP A 105 THR A 129 1 25
HELIX 5 5 SER A 139 HIS A 149 1 11
HELIX 6 6 THR A 156 PHE A 167 1 12
HELIX 7 7 PHE A 167 ALA A 172 1 6
HELIX 8 8 LEU A 186 GLY A 193 1 8
HELIX 9 9 GLU A 206 GLN A 215 1 10
HELIX 10 10 SER A 267 SER A 273 1 7
HELIX 11 11 PRO A 283 PHE A 293 1 11
HELIX 12 12 ASP A 351 GLN A 359 1 9
HELIX 13 13 SER A 361 PHE A 377 1 17
HELIX 14 14 ASN A 411 ALA A 420 1 10
HELIX 15 15 GLY A 429 SER A 433 5 5
HELIX 16 16 TYR A 439 GLN A 459 1 21
HELIX 17 17 GLY B 13 ALA B 26 1 14
HELIX 18 18 PRO B 71 SER B 78 1 8
HELIX 19 19 TYR B 91 GLN B 94 5 4
HELIX 20 20 ASP B 105 LEU B 130 1 26
HELIX 21 21 SER B 139 HIS B 149 1 11
HELIX 22 22 THR B 156 PHE B 167 1 12
HELIX 23 23 PHE B 167 ALA B 172 1 6
HELIX 24 24 SER B 179 VAL B 184 1 6
HELIX 25 25 LEU B 186 GLY B 193 1 8
HELIX 26 26 GLU B 206 GLN B 215 1 10
HELIX 27 27 SER B 267 GLN B 272 1 6
HELIX 28 28 PRO B 283 PHE B 293 1 11
HELIX 29 29 ASP B 351 GLN B 359 1 9
HELIX 30 30 SER B 361 PHE B 377 1 17
HELIX 31 31 ASN B 411 ALA B 420 1 10
HELIX 32 32 GLY B 429 SER B 433 5 5
HELIX 33 33 TYR B 439 LYS B 461 1 23
HELIX 34 34 GLY C 13 ALA C 26 1 14
HELIX 35 35 PRO C 71 SER C 78 1 8
HELIX 36 36 TYR C 91 GLN C 94 5 4
HELIX 37 37 ASP C 105 LEU C 130 1 26
HELIX 38 38 SER C 139 HIS C 149 1 11
HELIX 39 39 THR C 156 PHE C 167 1 12
HELIX 40 40 PHE C 167 ALA C 172 1 6
HELIX 41 41 LEU C 186 GLY C 193 1 8
HELIX 42 42 GLU C 206 GLY C 214 1 9
HELIX 43 43 SER C 267 SER C 273 1 7
HELIX 44 44 PRO C 283 PHE C 293 1 11
HELIX 45 45 ASP C 351 GLN C 359 1 9
HELIX 46 46 SER C 361 PHE C 377 1 17
HELIX 47 47 ASN C 411 ALA C 420 1 10
HELIX 48 48 GLY C 429 SER C 433 5 5
HELIX 49 49 TYR C 439 LYS C 461 1 23
SHEET 1 AA 5 LEU A 231 GLN A 232 0
SHEET 2 AA 5 LEU A 31 LEU A 34 1 O ILE A 33 N GLN A 232
SHEET 3 AA 5 VAL A 7 VAL A 10 1 O VAL A 7 N LEU A 32
SHEET 4 AA 5 TYR A 261 VAL A 264 1 O TYR A 261 N ILE A 8
SHEET 5 AA 5 VAL A 425 PHE A 427 1 O TYR A 426 N VAL A 264
SHEET 1 AB 2 LYS A 46 PHE A 49 0
SHEET 2 AB 2 ILE A 52 GLU A 55 -1 O ILE A 52 N PHE A 49
SHEET 1 AC 3 TRP A 60 VAL A 64 0
SHEET 2 AC 3 ASP A 195 VAL A 199 -1 O ASP A 195 N GLY A 63
SHEET 3 AC 3 ASN A 84 ARG A 86 -1 O PHE A 85 N PHE A 198
SHEET 1 AD 6 VAL A 96 LYS A 98 0
SHEET 2 AD 6 PHE A 318 ALA A 322 1 O LEU A 320 N TYR A 97
SHEET 3 AD 6 VAL A 331 GLU A 334 -1 O TRP A 332 N PHE A 319
SHEET 4 AD 6 VAL A 344 THR A 350 -1 O LEU A 346 N GLN A 333
SHEET 5 AD 6 TYR A 298 LYS A 304 -1 O THR A 299 N VAL A 349
SHEET 6 AD 6 ASP A 387 LEU A 389 -1 O ASP A 387 N LYS A 304
SHEET 1 AE 4 VAL A 256 ALA A 259 0
SHEET 2 AE 4 VAL A 247 THR A 251 -1 O VAL A 247 N ALA A 259
SHEET 3 AE 4 VAL A 237 TYR A 242 -1 N ARG A 238 O LYS A 250
SHEET 4 AE 4 GLN A 277 LYS A 279 1 O GLN A 277 N ILE A 240
SHEET 1 AF 2 ASP A 294 ALA A 296 0
SHEET 2 AF 2 PHE A 403 ASN A 405 -1 O PHE A 403 N ALA A 296
SHEET 1 BA 5 LEU B 231 GLN B 232 0
SHEET 2 BA 5 ASP B 30 LEU B 34 1 O ILE B 33 N GLN B 232
SHEET 3 BA 5 ARG B 6 VAL B 10 1 O VAL B 7 N LEU B 32
SHEET 4 BA 5 TYR B 261 VAL B 264 1 O TYR B 261 N ILE B 8
SHEET 5 BA 5 VAL B 425 PHE B 427 1 O TYR B 426 N VAL B 264
SHEET 1 BB 2 LYS B 46 PHE B 49 0
SHEET 2 BB 2 ILE B 52 GLU B 55 -1 O ILE B 52 N PHE B 49
SHEET 1 BC 3 TRP B 60 VAL B 64 0
SHEET 2 BC 3 ASP B 195 VAL B 199 -1 O ASP B 195 N GLY B 63
SHEET 3 BC 3 ASN B 84 ARG B 86 -1 O PHE B 85 N PHE B 198
SHEET 1 BD 6 VAL B 96 LYS B 98 0
SHEET 2 BD 6 PHE B 318 ALA B 322 1 O LEU B 320 N TYR B 97
SHEET 3 BD 6 VAL B 331 GLU B 334 -1 O TRP B 332 N PHE B 319
SHEET 4 BD 6 VAL B 344 THR B 350 -1 O LEU B 346 N GLN B 333
SHEET 5 BD 6 TYR B 298 LYS B 304 -1 O THR B 299 N VAL B 349
SHEET 6 BD 6 ASP B 387 LEU B 389 -1 O ASP B 387 N LYS B 304
SHEET 1 BE 4 VAL B 256 ALA B 259 0
SHEET 2 BE 4 VAL B 247 THR B 251 -1 O VAL B 247 N ALA B 259
SHEET 3 BE 4 VAL B 237 TYR B 242 -1 N ARG B 238 O LYS B 250
SHEET 4 BE 4 GLN B 277 LYS B 279 1 O GLN B 277 N ILE B 240
SHEET 1 BF 2 ASP B 294 ALA B 296 0
SHEET 2 BF 2 PHE B 403 ASN B 405 -1 O PHE B 403 N ALA B 296
SHEET 1 CA 5 LEU C 231 GLN C 232 0
SHEET 2 CA 5 LEU C 31 LEU C 34 1 O ILE C 33 N GLN C 232
SHEET 3 CA 5 VAL C 7 VAL C 10 1 O VAL C 7 N LEU C 32
SHEET 4 CA 5 TYR C 261 VAL C 264 1 O TYR C 261 N ILE C 8
SHEET 5 CA 5 VAL C 425 PHE C 427 1 O TYR C 426 N VAL C 264
SHEET 1 CB 2 LYS C 46 PHE C 49 0
SHEET 2 CB 2 ILE C 52 GLU C 55 -1 O ILE C 52 N PHE C 49
SHEET 1 CC 3 TRP C 60 VAL C 64 0
SHEET 2 CC 3 ASP C 195 VAL C 199 -1 O ASP C 195 N GLY C 63
SHEET 3 CC 3 ASN C 84 ARG C 86 -1 O PHE C 85 N PHE C 198
SHEET 1 CD 6 VAL C 96 LYS C 98 0
SHEET 2 CD 6 PHE C 318 ALA C 322 1 O LEU C 320 N TYR C 97
SHEET 3 CD 6 VAL C 331 GLU C 334 -1 O TRP C 332 N PHE C 319
SHEET 4 CD 6 VAL C 344 THR C 350 -1 O LEU C 346 N GLN C 333
SHEET 5 CD 6 TYR C 298 LYS C 304 -1 O THR C 299 N VAL C 349
SHEET 6 CD 6 ASP C 387 LEU C 389 -1 O ASP C 387 N LYS C 304
SHEET 1 CE 4 VAL C 256 ALA C 259 0
SHEET 2 CE 4 GLY C 246 THR C 251 -1 O VAL C 247 N ALA C 259
SHEET 3 CE 4 VAL C 237 SER C 243 -1 N ARG C 238 O LYS C 250
SHEET 4 CE 4 GLN C 277 LYS C 279 1 O GLN C 277 N ILE C 240
SHEET 1 CF 2 ASP C 294 ALA C 296 0
SHEET 2 CF 2 PHE C 403 ASN C 405 -1 O PHE C 403 N ALA C 296
SSBOND 1 CYS A 457 CYS A 463 1555 1555 2.04
SSBOND 2 CYS B 457 CYS B 463 1555 1555 2.02
SSBOND 3 CYS C 457 CYS C 463 1555 1555 2.04
LINK ND2 ASN A 77 C1 NAG D 1 1555 1555 1.40
LINK ND2 ASN B 77 C1 NAG E 1 1555 1555 1.41
LINK ND2 ASN C 77 C1 NAG F 1 1555 1555 1.42
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.81
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.79
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.70
LINK O3 NAG F 1 C1 FCA F 5 1555 1555 1.31
LINK O4 NAG F 2 C1 MAN F 3 1555 1555 1.09
LINK O6 MAN F 3 C1 MAN F 4 1555 1555 1.38
CISPEP 1 VAL A 184 PRO A 185 0 -2.52
CISPEP 2 LYS A 279 PRO A 280 0 -0.18
CISPEP 3 VAL B 184 PRO B 185 0 -0.85
CISPEP 4 LYS B 279 PRO B 280 0 -0.39
CISPEP 5 VAL C 184 PRO C 185 0 -4.26
CISPEP 6 LYS C 279 PRO C 280 0 2.44
CRYST1 181.770 181.770 277.530 90.00 90.00 120.00 P 65 2 2 36
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 0.005501 0.003176 0.000000 0.00000
SCALE2 0.000000 0.006352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003603 0.00000
MTRIX1 1 0.137894 -0.485816 0.863115 84.16400 1
MTRIX2 1 0.487082 0.792042 0.367994 -60.69300 1
MTRIX3 1 -0.862402 0.369664 0.345850 107.70600 1
MTRIX1 2 -0.387625 -0.912764 0.128873 189.07800 1
MTRIX2 2 -0.357429 0.019957 -0.933727 114.48400 1
MTRIX3 2 0.849701 -0.407999 -0.333984 -57.26700 1
(ATOM LINES ARE NOT SHOWN.)
END