HEADER LYASE 12-JUN-03 1PN4
TITLE CRYSTAL STRUCTURE OF 2-ENOYL-COA HYDRATASE 2 DOMAIN OF CANDIDA
TITLE 2 TROPICALIS MULTIFUNCTIONAL ENZYME TYPE 2 COMPLEXED WITH (3R)-
TITLE 3 HYDROXYDECANOYL-COA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOMAL HYDRATASE-DEHYDROGENASE-EPIMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: 2-ENOYL-COA HYDRATASE 2 DOMAIN;
COMPND 5 SYNONYM: HDE, MULTIFUNCTIONAL BETA-OXIDATION PROTEIN, MFP;
COMPND 6 EC: 4.2.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA TROPICALIS;
SOURCE 3 ORGANISM_TAXID: 5482;
SOURCE 4 GENE: FOX2;
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: PET3A
KEYWDS HOT-DOG FOLD, HYDRATASE 2 MOTIF, OXYANION HOLE, ENZYME-PRODUCT
KEYWDS 2 COMPLEX, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.KOSKI,A.M.HAAPALAINEN,J.K.HILTUNEN,T.GLUMOFF
REVDAT 6 16-AUG-23 1PN4 1 REMARK
REVDAT 5 27-OCT-21 1PN4 1 REMARK SEQADV
REVDAT 4 24-JUL-19 1PN4 1 REMARK
REVDAT 3 24-FEB-09 1PN4 1 VERSN
REVDAT 2 08-JUN-04 1PN4 1 JRNL
REVDAT 1 13-APR-04 1PN4 0
JRNL AUTH M.K.KOSKI,A.M.HAAPALAINEN,J.K.HILTUNEN,T.GLUMOFF
JRNL TITL A TWO-DOMAIN STRUCTURE OF ONE SUBUNIT EXPLAINS UNIQUE
JRNL TITL 2 FEATURES OF EUKARYOTIC HYDRATASE 2.
JRNL REF J.BIOL.CHEM. V. 279 24666 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15051722
JRNL DOI 10.1074/JBC.M400293200
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 47255
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2363
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8426
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 196
REMARK 3 SOLVENT ATOMS : 465
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.014 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.550 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8019
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, DENZO
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.23200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.530
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: SUBUNIT D OF PDB ENTRY 1PN2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, HEPES, TRANS-2-DECENOYL
REMARK 280 -COA, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 75.64500
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 300 REMARK: THE ASYMMETRIC UNIT IS COMPLETE AND THE BIOLOGICAL UNIT IS
REMARK 300 A DIMER.
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: 6070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 31.0 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: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 4
REMARK 465 LYS A 277
REMARK 465 ALA A 278
REMARK 465 LYS A 279
REMARK 465 ILE A 280
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
REMARK 465 ASP B 4
REMARK 465 LYS B 277
REMARK 465 ALA B 278
REMARK 465 LYS B 279
REMARK 465 ILE B 280
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASP C 3
REMARK 465 SER C 52
REMARK 465 GLY C 53
REMARK 465 LYS C 54
REMARK 465 SER C 55
REMARK 465 GLN C 56
REMARK 465 ASN C 57
REMARK 465 SER C 58
REMARK 465 PHE C 59
REMARK 465 ALA C 60
REMARK 465 LYS C 61
REMARK 465 LEU C 62
REMARK 465 LEU C 63
REMARK 465 ARG C 64
REMARK 465 ASN C 65
REMARK 465 PHE C 66
REMARK 465 ASN C 67
REMARK 465 PRO C 68
REMARK 465 MET C 69
REMARK 465 LEU C 70
REMARK 465 LEU C 71
REMARK 465 LYS C 103
REMARK 465 GLY C 104
REMARK 465 THR C 105
REMARK 465 ASN C 106
REMARK 465 GLY C 275
REMARK 465 ASP C 276
REMARK 465 LYS C 277
REMARK 465 ALA C 278
REMARK 465 LYS C 279
REMARK 465 ILE C 280
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 ASP D 3
REMARK 465 LYS D 277
REMARK 465 ALA D 278
REMARK 465 LYS D 279
REMARK 465 ILE D 280
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 54 CG CD CE NZ
REMARK 480 LYS A 92 CE NZ
REMARK 480 LYS A 141 CD CE NZ
REMARK 480 LYS A 158 CE NZ
REMARK 480 ASP A 276 CB CG OD1 OD2
REMARK 480 LYS B 26 CD CE NZ
REMARK 480 LYS B 54 CG CD CE NZ
REMARK 480 LYS B 92 CE NZ
REMARK 480 LYS B 114 CE NZ
REMARK 480 LYS B 119 CD CE NZ
REMARK 480 LYS B 158 CD CE NZ
REMARK 480 LYS B 197 NZ
REMARK 480 LYS B 200 CD CE NZ
REMARK 480 LYS B 246 NZ
REMARK 480 ASP B 249 CB CG OD1 OD2
REMARK 480 ASP B 250 CG OD1 OD2
REMARK 480 ARG C 8 CD NE CZ NH1 NH2
REMARK 480 LYS C 26 CE NZ
REMARK 480 LYS C 92 CE NZ
REMARK 480 PHE C 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 ILE C 133 CB CG1 CG2 CD1
REMARK 480 ARG C 134 CG CD NE CZ NH1 NH2
REMARK 480 ASN C 135 CG OD1 ND2
REMARK 480 GLN C 137 CB CG CD OE1 NE2
REMARK 480 ASP C 139 CG OD1 OD2
REMARK 480 LYS C 141 CG CD CE NZ
REMARK 480 LYS C 158 CB CG CD CE NZ
REMARK 480 LYS C 197 NZ
REMARK 480 LYS C 246 CE NZ
REMARK 480 ASP C 249 CG OD1 OD2
REMARK 480 LYS D 54 CG CD CE NZ
REMARK 480 LYS D 92 CE NZ
REMARK 480 LYS D 114 NZ
REMARK 480 LYS D 119 CG CD CE NZ
REMARK 480 LYS D 194 CD CE NZ
REMARK 480 LYS D 197 CD CE NZ
REMARK 480 LYS D 246 NZ
REMARK 480 ASP D 249 CG OD1 OD2
REMARK 480 ASP D 250 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS B 54 CB LYS B 54 CG -0.188
REMARK 500 LYS B 114 CD LYS B 114 CE -0.170
REMARK 500 LYS B 158 CG LYS B 158 CD -0.222
REMARK 500 ARG C 8 CG ARG C 8 CD -0.203
REMARK 500 LYS C 26 CD LYS C 26 CE -0.176
REMARK 500 PHE C 132 CB PHE C 132 CG 0.103
REMARK 500 ASN C 135 CB ASN C 135 CG 0.149
REMARK 500 LYS D 54 CB LYS D 54 CG -0.260
REMARK 500 LYS D 114 CE LYS D 114 NZ -0.155
REMARK 500 LYS D 119 CB LYS D 119 CG -0.178
REMARK 500 ASP D 250 CB ASP D 250 CG -0.185
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 ASP A 172 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 11 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 LYS B 54 CA - CB - CG ANGL. DEV. = 20.7 DEGREES
REMARK 500 ASP B 172 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 229 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP C 13 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLN C 137 CB - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 GLN C 137 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 ASP C 139 N - CA - C ANGL. DEV. = 23.9 DEGREES
REMARK 500 ASP C 145 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP C 172 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 249 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP C 249 CB - CG - OD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP C 250 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LYS D 194 CB - CG - CD ANGL. DEV. = 16.3 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 PHE A 154 58.27 36.41
REMARK 500 ASN A 184 124.30 -39.38
REMARK 500 LYS A 197 28.85 83.58
REMARK 500 ASN B 184 122.34 -38.01
REMARK 500 ILE B 188 -36.29 -131.21
REMARK 500 GLN C 137 66.47 17.62
REMARK 500 ASP C 139 171.71 -40.19
REMARK 500 ILE C 188 -39.70 -144.39
REMARK 500 SER D 248 -179.86 179.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HDC D 3277
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDC A 1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDC B 2277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDC D 3277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PN2 RELATED DB: PDB
REMARK 900 THE APO FORM OF THE SAME PROTEIN.
DBREF 1PN4 A 1 280 UNP P22414 FOX2_CANTR 627 906
DBREF 1PN4 B 1 280 UNP P22414 FOX2_CANTR 627 906
DBREF 1PN4 C 1 280 UNP P22414 FOX2_CANTR 627 906
DBREF 1PN4 D 1 280 UNP P22414 FOX2_CANTR 627 906
SEQADV 1PN4 MET A 1 UNP P22414 GLU 627 ENGINEERED MUTATION
SEQADV 1PN4 GLN A 187 UNP P22414 HIS 813 ENGINEERED MUTATION
SEQADV 1PN4 MET B 1 UNP P22414 GLU 627 ENGINEERED MUTATION
SEQADV 1PN4 GLN B 187 UNP P22414 HIS 813 ENGINEERED MUTATION
SEQADV 1PN4 MET C 1 UNP P22414 GLU 627 ENGINEERED MUTATION
SEQADV 1PN4 GLN C 187 UNP P22414 HIS 813 ENGINEERED MUTATION
SEQADV 1PN4 MET D 1 UNP P22414 GLU 627 ENGINEERED MUTATION
SEQADV 1PN4 GLN D 187 UNP P22414 HIS 813 ENGINEERED MUTATION
SEQRES 1 A 280 MET GLU ASP ASP PRO VAL TRP ARG PHE ASP ASP ARG ASP
SEQRES 2 A 280 VAL ILE LEU TYR ASN ILE ALA LEU GLY ALA THR THR LYS
SEQRES 3 A 280 GLN LEU LYS TYR VAL TYR GLU ASN ASP SER ASP PHE GLN
SEQRES 4 A 280 VAL ILE PRO THR PHE GLY HIS LEU ILE THR PHE ASN SER
SEQRES 5 A 280 GLY LYS SER GLN ASN SER PHE ALA LYS LEU LEU ARG ASN
SEQRES 6 A 280 PHE ASN PRO MET LEU LEU LEU HIS GLY GLU HIS TYR LEU
SEQRES 7 A 280 LYS VAL HIS SER TRP PRO PRO PRO THR GLU GLY GLU ILE
SEQRES 8 A 280 LYS THR THR PHE GLU PRO ILE ALA THR THR PRO LYS GLY
SEQRES 9 A 280 THR ASN VAL VAL ILE VAL HIS GLY SER LYS SER VAL ASP
SEQRES 10 A 280 ASN LYS SER GLY GLU LEU ILE TYR SER ASN GLU ALA THR
SEQRES 11 A 280 TYR PHE ILE ARG ASN CYS GLN ALA ASP ASN LYS VAL TYR
SEQRES 12 A 280 ALA ASP ARG PRO ALA PHE ALA THR ASN GLN PHE LEU ALA
SEQRES 13 A 280 PRO LYS ARG ALA PRO ASP TYR GLN VAL ASP VAL PRO VAL
SEQRES 14 A 280 SER GLU ASP LEU ALA ALA LEU TYR ARG LEU SER GLY ASP
SEQRES 15 A 280 ARG ASN PRO LEU GLN ILE ASP PRO ASN PHE ALA LYS GLY
SEQRES 16 A 280 ALA LYS PHE PRO LYS PRO ILE LEU HIS GLY MET CYS THR
SEQRES 17 A 280 TYR GLY LEU SER ALA LYS ALA LEU ILE ASP LYS PHE GLY
SEQRES 18 A 280 MET PHE ASN GLU ILE LYS ALA ARG PHE THR GLY ILE VAL
SEQRES 19 A 280 PHE PRO GLY GLU THR LEU ARG VAL LEU ALA TRP LYS GLU
SEQRES 20 A 280 SER ASP ASP THR ILE VAL PHE GLN THR HIS VAL VAL ASP
SEQRES 21 A 280 ARG GLY THR ILE ALA ILE ASN ASN ALA ALA ILE LYS LEU
SEQRES 22 A 280 VAL GLY ASP LYS ALA LYS ILE
SEQRES 1 B 280 MET GLU ASP ASP PRO VAL TRP ARG PHE ASP ASP ARG ASP
SEQRES 2 B 280 VAL ILE LEU TYR ASN ILE ALA LEU GLY ALA THR THR LYS
SEQRES 3 B 280 GLN LEU LYS TYR VAL TYR GLU ASN ASP SER ASP PHE GLN
SEQRES 4 B 280 VAL ILE PRO THR PHE GLY HIS LEU ILE THR PHE ASN SER
SEQRES 5 B 280 GLY LYS SER GLN ASN SER PHE ALA LYS LEU LEU ARG ASN
SEQRES 6 B 280 PHE ASN PRO MET LEU LEU LEU HIS GLY GLU HIS TYR LEU
SEQRES 7 B 280 LYS VAL HIS SER TRP PRO PRO PRO THR GLU GLY GLU ILE
SEQRES 8 B 280 LYS THR THR PHE GLU PRO ILE ALA THR THR PRO LYS GLY
SEQRES 9 B 280 THR ASN VAL VAL ILE VAL HIS GLY SER LYS SER VAL ASP
SEQRES 10 B 280 ASN LYS SER GLY GLU LEU ILE TYR SER ASN GLU ALA THR
SEQRES 11 B 280 TYR PHE ILE ARG ASN CYS GLN ALA ASP ASN LYS VAL TYR
SEQRES 12 B 280 ALA ASP ARG PRO ALA PHE ALA THR ASN GLN PHE LEU ALA
SEQRES 13 B 280 PRO LYS ARG ALA PRO ASP TYR GLN VAL ASP VAL PRO VAL
SEQRES 14 B 280 SER GLU ASP LEU ALA ALA LEU TYR ARG LEU SER GLY ASP
SEQRES 15 B 280 ARG ASN PRO LEU GLN ILE ASP PRO ASN PHE ALA LYS GLY
SEQRES 16 B 280 ALA LYS PHE PRO LYS PRO ILE LEU HIS GLY MET CYS THR
SEQRES 17 B 280 TYR GLY LEU SER ALA LYS ALA LEU ILE ASP LYS PHE GLY
SEQRES 18 B 280 MET PHE ASN GLU ILE LYS ALA ARG PHE THR GLY ILE VAL
SEQRES 19 B 280 PHE PRO GLY GLU THR LEU ARG VAL LEU ALA TRP LYS GLU
SEQRES 20 B 280 SER ASP ASP THR ILE VAL PHE GLN THR HIS VAL VAL ASP
SEQRES 21 B 280 ARG GLY THR ILE ALA ILE ASN ASN ALA ALA ILE LYS LEU
SEQRES 22 B 280 VAL GLY ASP LYS ALA LYS ILE
SEQRES 1 C 280 MET GLU ASP ASP PRO VAL TRP ARG PHE ASP ASP ARG ASP
SEQRES 2 C 280 VAL ILE LEU TYR ASN ILE ALA LEU GLY ALA THR THR LYS
SEQRES 3 C 280 GLN LEU LYS TYR VAL TYR GLU ASN ASP SER ASP PHE GLN
SEQRES 4 C 280 VAL ILE PRO THR PHE GLY HIS LEU ILE THR PHE ASN SER
SEQRES 5 C 280 GLY LYS SER GLN ASN SER PHE ALA LYS LEU LEU ARG ASN
SEQRES 6 C 280 PHE ASN PRO MET LEU LEU LEU HIS GLY GLU HIS TYR LEU
SEQRES 7 C 280 LYS VAL HIS SER TRP PRO PRO PRO THR GLU GLY GLU ILE
SEQRES 8 C 280 LYS THR THR PHE GLU PRO ILE ALA THR THR PRO LYS GLY
SEQRES 9 C 280 THR ASN VAL VAL ILE VAL HIS GLY SER LYS SER VAL ASP
SEQRES 10 C 280 ASN LYS SER GLY GLU LEU ILE TYR SER ASN GLU ALA THR
SEQRES 11 C 280 TYR PHE ILE ARG ASN CYS GLN ALA ASP ASN LYS VAL TYR
SEQRES 12 C 280 ALA ASP ARG PRO ALA PHE ALA THR ASN GLN PHE LEU ALA
SEQRES 13 C 280 PRO LYS ARG ALA PRO ASP TYR GLN VAL ASP VAL PRO VAL
SEQRES 14 C 280 SER GLU ASP LEU ALA ALA LEU TYR ARG LEU SER GLY ASP
SEQRES 15 C 280 ARG ASN PRO LEU GLN ILE ASP PRO ASN PHE ALA LYS GLY
SEQRES 16 C 280 ALA LYS PHE PRO LYS PRO ILE LEU HIS GLY MET CYS THR
SEQRES 17 C 280 TYR GLY LEU SER ALA LYS ALA LEU ILE ASP LYS PHE GLY
SEQRES 18 C 280 MET PHE ASN GLU ILE LYS ALA ARG PHE THR GLY ILE VAL
SEQRES 19 C 280 PHE PRO GLY GLU THR LEU ARG VAL LEU ALA TRP LYS GLU
SEQRES 20 C 280 SER ASP ASP THR ILE VAL PHE GLN THR HIS VAL VAL ASP
SEQRES 21 C 280 ARG GLY THR ILE ALA ILE ASN ASN ALA ALA ILE LYS LEU
SEQRES 22 C 280 VAL GLY ASP LYS ALA LYS ILE
SEQRES 1 D 280 MET GLU ASP ASP PRO VAL TRP ARG PHE ASP ASP ARG ASP
SEQRES 2 D 280 VAL ILE LEU TYR ASN ILE ALA LEU GLY ALA THR THR LYS
SEQRES 3 D 280 GLN LEU LYS TYR VAL TYR GLU ASN ASP SER ASP PHE GLN
SEQRES 4 D 280 VAL ILE PRO THR PHE GLY HIS LEU ILE THR PHE ASN SER
SEQRES 5 D 280 GLY LYS SER GLN ASN SER PHE ALA LYS LEU LEU ARG ASN
SEQRES 6 D 280 PHE ASN PRO MET LEU LEU LEU HIS GLY GLU HIS TYR LEU
SEQRES 7 D 280 LYS VAL HIS SER TRP PRO PRO PRO THR GLU GLY GLU ILE
SEQRES 8 D 280 LYS THR THR PHE GLU PRO ILE ALA THR THR PRO LYS GLY
SEQRES 9 D 280 THR ASN VAL VAL ILE VAL HIS GLY SER LYS SER VAL ASP
SEQRES 10 D 280 ASN LYS SER GLY GLU LEU ILE TYR SER ASN GLU ALA THR
SEQRES 11 D 280 TYR PHE ILE ARG ASN CYS GLN ALA ASP ASN LYS VAL TYR
SEQRES 12 D 280 ALA ASP ARG PRO ALA PHE ALA THR ASN GLN PHE LEU ALA
SEQRES 13 D 280 PRO LYS ARG ALA PRO ASP TYR GLN VAL ASP VAL PRO VAL
SEQRES 14 D 280 SER GLU ASP LEU ALA ALA LEU TYR ARG LEU SER GLY ASP
SEQRES 15 D 280 ARG ASN PRO LEU GLN ILE ASP PRO ASN PHE ALA LYS GLY
SEQRES 16 D 280 ALA LYS PHE PRO LYS PRO ILE LEU HIS GLY MET CYS THR
SEQRES 17 D 280 TYR GLY LEU SER ALA LYS ALA LEU ILE ASP LYS PHE GLY
SEQRES 18 D 280 MET PHE ASN GLU ILE LYS ALA ARG PHE THR GLY ILE VAL
SEQRES 19 D 280 PHE PRO GLY GLU THR LEU ARG VAL LEU ALA TRP LYS GLU
SEQRES 20 D 280 SER ASP ASP THR ILE VAL PHE GLN THR HIS VAL VAL ASP
SEQRES 21 D 280 ARG GLY THR ILE ALA ILE ASN ASN ALA ALA ILE LYS LEU
SEQRES 22 D 280 VAL GLY ASP LYS ALA LYS ILE
HET HDC A1277 60
HET EDO A 504 4
HET HDC B2277 60
HET EDO B 501 4
HET EDO B 502 4
HET EDO B 503 4
HET HDC D3277 60
HETNAM HDC 3R-HYDROXYDECANOYL-COENZYME A
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HDC 3R-HYDROXYDECANOYL-COA
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 HDC 3(C31 H54 N7 O18 P3 S)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 12 HOH *465(H2 O)
HELIX 1 1 ASP A 10 LEU A 21 1 12
HELIX 2 2 THR A 24 LYS A 26 5 3
HELIX 3 3 GLN A 27 TYR A 32 1 6
HELIX 4 4 ILE A 41 HIS A 46 5 6
HELIX 5 5 LEU A 47 SER A 52 1 6
HELIX 6 6 GLY A 53 LEU A 63 5 11
HELIX 7 7 ASN A 67 MET A 69 5 3
HELIX 8 8 PRO A 147 ASN A 152 1 6
HELIX 9 9 ASP A 172 ARG A 178 1 7
HELIX 10 10 LEU A 179 GLY A 181 5 3
HELIX 11 11 ASN A 184 ILE A 188 5 5
HELIX 12 12 ASP A 189 ALA A 196 1 8
HELIX 13 13 HIS A 204 GLY A 221 1 18
HELIX 14 14 ASP B 10 LEU B 21 1 12
HELIX 15 15 GLN B 27 TYR B 32 1 6
HELIX 16 16 ILE B 41 PHE B 50 5 10
HELIX 17 17 GLY B 53 LEU B 63 5 11
HELIX 18 18 ASN B 67 MET B 69 5 3
HELIX 19 19 PRO B 147 ASN B 152 1 6
HELIX 20 20 ASP B 172 ARG B 178 1 7
HELIX 21 21 LEU B 179 GLY B 181 5 3
HELIX 22 22 ASN B 184 ILE B 188 5 5
HELIX 23 23 ASP B 189 ALA B 196 1 8
HELIX 24 24 HIS B 204 GLY B 221 1 18
HELIX 25 25 ASP C 10 LEU C 21 1 12
HELIX 26 26 GLN C 27 TYR C 32 1 6
HELIX 27 27 ILE C 41 PHE C 50 5 10
HELIX 28 28 PRO C 147 ASN C 152 1 6
HELIX 29 29 ASP C 172 ARG C 178 1 7
HELIX 30 30 LEU C 179 GLY C 181 5 3
HELIX 31 31 ASN C 184 ILE C 188 5 5
HELIX 32 32 ASP C 189 ALA C 196 1 8
HELIX 33 33 HIS C 204 GLY C 221 1 18
HELIX 34 34 ASP D 10 LEU D 21 1 12
HELIX 35 35 GLN D 27 TYR D 32 1 6
HELIX 36 36 ILE D 41 HIS D 46 5 6
HELIX 37 37 LEU D 47 SER D 52 1 6
HELIX 38 38 GLY D 53 LYS D 61 5 9
HELIX 39 39 ASN D 67 MET D 69 5 3
HELIX 40 40 PRO D 147 ASN D 152 1 6
HELIX 41 41 ASP D 172 ARG D 178 1 7
HELIX 42 42 LEU D 179 GLY D 181 5 3
HELIX 43 43 ASN D 184 ILE D 188 5 5
HELIX 44 44 ASP D 189 ALA D 196 1 8
HELIX 45 45 HIS D 204 GLY D 221 1 18
SHEET 1 A 3 VAL A 6 PHE A 9 0
SHEET 2 A 3 GLY A 89 LYS A 103 -1 O ILE A 91 N TRP A 7
SHEET 3 A 3 LYS A 141 VAL A 142 -1 O LYS A 141 N THR A 100
SHEET 1 B10 VAL A 6 PHE A 9 0
SHEET 2 B10 GLY A 89 LYS A 103 -1 O ILE A 91 N TRP A 7
SHEET 3 B10 ASN A 106 ASP A 117 -1 O VAL A 110 N ALA A 99
SHEET 4 B10 LEU A 123 ILE A 133 -1 O ALA A 129 N HIS A 111
SHEET 5 B10 LEU A 71 VAL A 80 -1 N LEU A 72 O PHE A 132
SHEET 6 B10 PHE A 223 PHE A 230 -1 O ILE A 226 N LEU A 78
SHEET 7 B10 THR A 263 LEU A 273 -1 O ASN A 267 N ARG A 229
SHEET 8 B10 THR A 251 VAL A 258 -1 N PHE A 254 O ALA A 269
SHEET 9 B10 THR A 239 LYS A 246 -1 N TRP A 245 O VAL A 253
SHEET 10 B10 TYR A 163 PRO A 168 -1 N TYR A 163 O ALA A 244
SHEET 1 C 3 VAL B 6 PHE B 9 0
SHEET 2 C 3 GLY B 89 LYS B 103 -1 O ILE B 91 N TRP B 7
SHEET 3 C 3 LYS B 141 VAL B 142 -1 O LYS B 141 N THR B 100
SHEET 1 D10 VAL B 6 PHE B 9 0
SHEET 2 D10 GLY B 89 LYS B 103 -1 O ILE B 91 N TRP B 7
SHEET 3 D10 ASN B 106 ASP B 117 -1 O GLY B 112 N GLU B 96
SHEET 4 D10 LEU B 123 ILE B 133 -1 O ALA B 129 N HIS B 111
SHEET 5 D10 LEU B 71 VAL B 80 -1 N GLU B 75 O THR B 130
SHEET 6 D10 PHE B 223 PHE B 230 -1 O ILE B 226 N LEU B 78
SHEET 7 D10 THR B 263 LEU B 273 -1 O LYS B 272 N GLU B 225
SHEET 8 D10 THR B 251 VAL B 258 -1 N THR B 256 O ILE B 266
SHEET 9 D10 THR B 239 LYS B 246 -1 N ARG B 241 O HIS B 257
SHEET 10 D10 TYR B 163 PRO B 168 -1 N VAL B 167 O LEU B 240
SHEET 1 E 3 VAL C 6 PHE C 9 0
SHEET 2 E 3 GLY C 89 THR C 101 -1 O ILE C 91 N TRP C 7
SHEET 3 E 3 LYS C 141 VAL C 142 -1 O LYS C 141 N THR C 100
SHEET 1 F10 VAL C 6 PHE C 9 0
SHEET 2 F10 GLY C 89 THR C 101 -1 O ILE C 91 N TRP C 7
SHEET 3 F10 VAL C 108 ASP C 117 -1 O VAL C 116 N LYS C 92
SHEET 4 F10 LEU C 123 PHE C 132 -1 O TYR C 131 N ILE C 109
SHEET 5 F10 HIS C 73 VAL C 80 -1 N GLU C 75 O THR C 130
SHEET 6 F10 PHE C 223 PHE C 230 -1 O ILE C 226 N LEU C 78
SHEET 7 F10 THR C 263 LEU C 273 -1 O LYS C 272 N GLU C 225
SHEET 8 F10 THR C 251 VAL C 258 -1 N THR C 256 O ILE C 266
SHEET 9 F10 THR C 239 LYS C 246 -1 N LEU C 243 O GLN C 255
SHEET 10 F10 TYR C 163 PRO C 168 -1 N VAL C 165 O VAL C 242
SHEET 1 G 3 VAL D 6 PHE D 9 0
SHEET 2 G 3 GLY D 89 LYS D 103 -1 O ILE D 91 N TRP D 7
SHEET 3 G 3 LYS D 141 VAL D 142 -1 O LYS D 141 N THR D 100
SHEET 1 H10 VAL D 6 PHE D 9 0
SHEET 2 H10 GLY D 89 LYS D 103 -1 O ILE D 91 N TRP D 7
SHEET 3 H10 ASN D 106 ASP D 117 -1 O VAL D 110 N ALA D 99
SHEET 4 H10 LEU D 123 ILE D 133 -1 O ALA D 129 N HIS D 111
SHEET 5 H10 LEU D 71 VAL D 80 -1 N GLU D 75 O THR D 130
SHEET 6 H10 PHE D 223 PHE D 230 -1 O ILE D 226 N LEU D 78
SHEET 7 H10 THR D 263 LEU D 273 -1 O ASN D 267 N ARG D 229
SHEET 8 H10 THR D 251 VAL D 258 -1 N PHE D 254 O ALA D 269
SHEET 9 H10 LEU D 240 LYS D 246 -1 N LEU D 243 O GLN D 255
SHEET 10 H10 TYR D 163 VAL D 167 -1 N VAL D 165 O VAL D 242
SHEET 1 I 2 LEU D 63 ARG D 64 0
SHEET 2 I 2 GLN D 137 ALA D 138 -1 O GLN D 137 N ARG D 64
CISPEP 1 TRP A 83 PRO A 84 0 -4.94
CISPEP 2 TRP B 83 PRO B 84 0 -2.91
CISPEP 3 TRP C 83 PRO C 84 0 -7.39
CISPEP 4 TRP D 83 PRO D 84 0 -7.32
SITE 1 AC1 22 ASN A 57 LEU A 71 LEU A 72 HIS A 73
SITE 2 AC1 22 GLY A 74 LYS A 103 TYR A 131 PHE A 132
SITE 3 AC1 22 ASP A 182 ASN A 184 GLN A 187 HIS A 204
SITE 4 AC1 22 GLY A 205 ARG A 229 PHE A 230 THR A 231
SITE 5 AC1 22 GLY A 232 ILE A 233 EDO A 504 HOH A1278
SITE 6 AC1 22 HOH A1336 HOH A1408
SITE 1 AC2 26 THR B 49 GLN B 56 ASN B 57 LEU B 71
SITE 2 AC2 26 HIS B 73 GLY B 74 GLU B 75 LYS B 103
SITE 3 AC2 26 TYR B 131 PHE B 132 ASP B 182 ASN B 184
SITE 4 AC2 26 GLN B 187 ILE B 202 HIS B 204 GLY B 205
SITE 5 AC2 26 ARG B 229 PHE B 230 THR B 231 GLY B 232
SITE 6 AC2 26 ILE B 233 EDO B 501 HOH B2304 HOH B2306
SITE 7 AC2 26 HOH B2406 HOH B2407
SITE 1 AC3 17 HIS D 73 GLY D 74 GLU D 75 LYS D 103
SITE 2 AC3 17 VAL D 108 PHE D 132 ASP D 182 ASN D 184
SITE 3 AC3 17 GLN D 187 GLY D 205 ARG D 229 PHE D 230
SITE 4 AC3 17 THR D 231 GLY D 232 ILE D 233 HOH D3283
SITE 5 AC3 17 HOH D3299
SITE 1 AC4 5 PRO B 68 ASN B 184 HDC B2277 HOH B2295
SITE 2 AC4 5 HOH B2316
SITE 1 AC5 5 GLU B 75 THR B 151 ASN B 152 GLN B 153
SITE 2 AC5 5 LYS B 227
SITE 1 AC6 2 GLN B 56 ASN B 57
SITE 1 AC7 5 PRO A 68 ASN A 184 HDC A1277 HOH A1311
SITE 2 AC7 5 HOH A1339
CRYST1 48.640 151.290 81.620 90.00 90.50 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 0.020559 0.000000 0.000179 0.00000
SCALE2 0.000000 0.006610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
