HEADER OXIDOREDUCTASE 16-JAN-07 2OK8
TITLE FERREDOXIN-NADP+ REDUCTASE FROM PLASMODIUM FALCIPARUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE FERREDOXIN--NADP REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FERREDOXIN--NADP REDUCTASE, PUTATIVE;
COMPND 5 EC: 1.18.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: ISOLATE 3D7;
SOURCE 5 GENE: ORF PFF1115W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DISULFIDE-STABILIZED DIMER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MILANI,E.MASTRANGELO,M.BOLOGNESI
REVDAT 5 27-DEC-23 2OK8 1 REMARK
REVDAT 4 06-AUG-14 2OK8 1 AUTHOR VERSN
REVDAT 3 24-FEB-09 2OK8 1 VERSN
REVDAT 2 13-MAR-07 2OK8 1 JRNL
REVDAT 1 13-FEB-07 2OK8 0
JRNL AUTH M.MILANI,E.BALCONI,A.ALIVERTI,E.MASTRANGELO,F.SEEBER,
JRNL AUTH 2 M.BOLOGNESI,G.ZANETTI
JRNL TITL FERREDOXIN-NADP(+) REDUCTASE FROM PLASMODIUM FALCIPARUM
JRNL TITL 2 UNDERGOES NADP(+)-DEPENDENT DIMERIZATION AND INACTIVATION:
JRNL TITL 3 FUNCTIONAL AND CRYSTALLOGRAPHIC ANALYSIS.
JRNL REF J.MOL.BIOL. V. 367 501 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17258767
JRNL DOI 10.1016/J.JMB.2007.01.005
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 60066
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3191
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4381
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 221
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 238
REMARK 3 SOLVENT ATOMS : 291
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.43000
REMARK 3 B12 (A**2) : -0.14000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.303
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.236
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 : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9208 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12474 ; 1.347 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1027 ; 6.379 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 466 ;38.057 ;24.442
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1564 ;16.940 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;22.945 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1304 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6950 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4012 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6165 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 453 ; 0.150 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 81 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.182 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5187 ; 2.067 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8418 ; 3.689 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4021 ; 4.594 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4056 ; 6.714 ; 6.000
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63426
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.48900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NH4 ACETATE 0.2 M, PEG 4000 22 % , PH
REMARK 280 5.4, MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 98.24133
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 49.12067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.12067
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 98.24133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 ASN A 4
REMARK 465 LEU A 63
REMARK 465 ASP A 64
REMARK 465 ASN A 65
REMARK 465 ASN A 66
REMARK 465 PRO A 67
REMARK 465 ASN A 68
REMARK 465 ASN A 69
REMARK 465 GLN A 70
REMARK 465 ILE A 71
REMARK 465 ASN A 72
REMARK 465 LYS A 73
REMARK 465 ASP A 74
REMARK 465 HIS A 75
REMARK 465 ASN A 76
REMARK 465 ILE A 77
REMARK 465 ILE A 78
REMARK 465 ASN A 79
REMARK 465 THR A 80
REMARK 465 THR A 81
REMARK 465 ASN A 82
REMARK 465 HIS A 83
REMARK 465 THR A 84
REMARK 465 ASN A 85
REMARK 465 HIS A 86
REMARK 465 ASN A 87
REMARK 465 ASN A 88
REMARK 465 ILE A 89
REMARK 465 ALA A 90
REMARK 465 LEU A 91
REMARK 465 SER A 92
REMARK 465 HIS A 93
REMARK 465 ILE A 94
REMARK 465 LYS A 95
REMARK 465 LYS A 96
REMARK 465 GLN A 97
REMARK 465 GLN A 125
REMARK 465 THR A 126
REMARK 465 GLU A 127
REMARK 465 ASN A 128
REMARK 465 ALA A 129
REMARK 465 PRO A 130
REMARK 465 ASN A 131
REMARK 465 ILE A 132
REMARK 465 LYS A 197
REMARK 465 ASN A 198
REMARK 465 ASN A 199
REMARK 465 LEU A 200
REMARK 465 TYR A 201
REMARK 465 ASN A 202
REMARK 465 LYS B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 ASN B 4
REMARK 465 ASP B 64
REMARK 465 ASN B 65
REMARK 465 ASN B 66
REMARK 465 PRO B 67
REMARK 465 ASN B 68
REMARK 465 ASN B 69
REMARK 465 GLN B 70
REMARK 465 ILE B 71
REMARK 465 ASN B 72
REMARK 465 LYS B 73
REMARK 465 ASP B 74
REMARK 465 HIS B 75
REMARK 465 ASN B 76
REMARK 465 ILE B 77
REMARK 465 ILE B 78
REMARK 465 ASN B 79
REMARK 465 THR B 80
REMARK 465 THR B 81
REMARK 465 ASN B 82
REMARK 465 HIS B 83
REMARK 465 THR B 84
REMARK 465 ASN B 85
REMARK 465 HIS B 86
REMARK 465 ASN B 87
REMARK 465 ASN B 88
REMARK 465 ILE B 89
REMARK 465 ALA B 90
REMARK 465 LEU B 91
REMARK 465 SER B 92
REMARK 465 HIS B 93
REMARK 465 ILE B 94
REMARK 465 LYS B 95
REMARK 465 LYS B 96
REMARK 465 GLN B 97
REMARK 465 THR B 126
REMARK 465 GLU B 127
REMARK 465 ASN B 128
REMARK 465 ALA B 129
REMARK 465 PRO B 130
REMARK 465 ASN B 131
REMARK 465 TYR B 195
REMARK 465 ASP B 196
REMARK 465 LYS B 197
REMARK 465 ASN B 198
REMARK 465 ASN B 199
REMARK 465 LEU B 200
REMARK 465 TYR B 201
REMARK 465 ASN B 202
REMARK 465 ARG B 203
REMARK 465 ASN B 204
REMARK 465 LYS C 1
REMARK 465 GLU C 2
REMARK 465 GLU C 3
REMARK 465 ASN C 4
REMARK 465 GLU C 62
REMARK 465 LEU C 63
REMARK 465 ASP C 64
REMARK 465 ASN C 65
REMARK 465 ASN C 66
REMARK 465 PRO C 67
REMARK 465 ASN C 68
REMARK 465 ASN C 69
REMARK 465 GLN C 70
REMARK 465 ILE C 71
REMARK 465 ASN C 72
REMARK 465 LYS C 73
REMARK 465 ASP C 74
REMARK 465 HIS C 75
REMARK 465 ASN C 76
REMARK 465 ILE C 77
REMARK 465 ILE C 78
REMARK 465 ASN C 79
REMARK 465 THR C 80
REMARK 465 THR C 81
REMARK 465 ASN C 82
REMARK 465 HIS C 83
REMARK 465 THR C 84
REMARK 465 ASN C 85
REMARK 465 HIS C 86
REMARK 465 ASN C 87
REMARK 465 ASN C 88
REMARK 465 ILE C 89
REMARK 465 ALA C 90
REMARK 465 LEU C 91
REMARK 465 SER C 92
REMARK 465 HIS C 93
REMARK 465 ILE C 94
REMARK 465 LYS C 95
REMARK 465 LYS C 96
REMARK 465 GLN C 97
REMARK 465 GLN C 125
REMARK 465 THR C 126
REMARK 465 GLU C 127
REMARK 465 ASN C 128
REMARK 465 ALA C 129
REMARK 465 PRO C 130
REMARK 465 ASN C 131
REMARK 465 ILE C 132
REMARK 465 ASP C 196
REMARK 465 LYS C 197
REMARK 465 ASN C 198
REMARK 465 ASN C 199
REMARK 465 LEU C 200
REMARK 465 TYR C 201
REMARK 465 ASN C 202
REMARK 465 ARG C 203
REMARK 465 HIS C 300
REMARK 465 ASP C 301
REMARK 465 GLN C 302
REMARK 465 LYS D 1
REMARK 465 GLU D 2
REMARK 465 GLU D 3
REMARK 465 ASN D 4
REMARK 465 LEU D 63
REMARK 465 ASP D 64
REMARK 465 ASN D 65
REMARK 465 ASN D 66
REMARK 465 PRO D 67
REMARK 465 ASN D 68
REMARK 465 ASN D 69
REMARK 465 GLN D 70
REMARK 465 ILE D 71
REMARK 465 ASN D 72
REMARK 465 LYS D 73
REMARK 465 ASP D 74
REMARK 465 HIS D 75
REMARK 465 ASN D 76
REMARK 465 ILE D 77
REMARK 465 ILE D 78
REMARK 465 ASN D 79
REMARK 465 THR D 80
REMARK 465 THR D 81
REMARK 465 ASN D 82
REMARK 465 HIS D 83
REMARK 465 THR D 84
REMARK 465 ASN D 85
REMARK 465 HIS D 86
REMARK 465 ASN D 87
REMARK 465 ASN D 88
REMARK 465 ILE D 89
REMARK 465 ALA D 90
REMARK 465 LEU D 91
REMARK 465 SER D 92
REMARK 465 HIS D 93
REMARK 465 ILE D 94
REMARK 465 LYS D 95
REMARK 465 LYS D 96
REMARK 465 GLN D 97
REMARK 465 GLU D 124
REMARK 465 GLN D 125
REMARK 465 THR D 126
REMARK 465 GLU D 127
REMARK 465 ASN D 128
REMARK 465 ALA D 129
REMARK 465 PRO D 130
REMARK 465 ASN D 131
REMARK 465 ILE D 132
REMARK 465 THR D 133
REMARK 465 LYS D 197
REMARK 465 ASN D 198
REMARK 465 ASN D 199
REMARK 465 SER D 299
REMARK 465 HIS D 300
REMARK 465 ASP D 301
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 ASN D 204 CG OD1 ND2
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 B 9031 O HOH B 9047 2.19
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 ASN A 148 -4.70 80.17
REMARK 500 ALA A 194 71.07 37.37
REMARK 500 ASN B 148 -2.89 80.52
REMARK 500 ALA B 156 112.62 51.58
REMARK 500 PHE B 303 82.33 52.61
REMARK 500 TYR C 59 17.60 55.66
REMARK 500 ASN C 134 93.04 70.40
REMARK 500 ASN C 148 -4.79 84.20
REMARK 500 LYS C 298 44.47 -97.63
REMARK 500 ASP C 304 -150.22 -80.45
REMARK 500 PRO D 29 -40.17 -26.20
REMARK 500 TYR D 59 5.29 59.24
REMARK 500 ASN D 148 2.84 84.67
REMARK 500 ALA D 166 -73.37 -16.27
REMARK 500 TYR D 201 139.60 -179.86
REMARK 500 ARG D 203 40.40 -101.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 154 GLY B 155 -134.76
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 FLC B 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 415
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OK7 RELATED DB: PDB
DBREF 2OK8 A 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK8 B 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK8 C 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK8 D 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
SEQRES 1 A 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 A 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 A 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 A 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 A 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 A 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 A 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 A 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 A 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 A 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 A 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 A 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 A 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 A 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 A 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 A 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 A 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 A 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 A 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 A 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 A 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 A 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 A 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 A 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 A 316 VAL GLU VAL TYR
SEQRES 1 B 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 B 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 B 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 B 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 B 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 B 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 B 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 B 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 B 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 B 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 B 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 B 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 B 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 B 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 B 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 B 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 B 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 B 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 B 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 B 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 B 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 B 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 B 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 B 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 B 316 VAL GLU VAL TYR
SEQRES 1 C 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 C 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 C 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 C 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 C 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 C 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 C 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 C 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 C 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 C 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 C 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 C 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 C 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 C 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 C 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 C 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 C 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 C 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 C 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 C 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 C 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 C 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 C 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 C 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 C 316 VAL GLU VAL TYR
SEQRES 1 D 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 D 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 D 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 D 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 D 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 D 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 D 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 D 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 D 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 D 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 D 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 D 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 D 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 D 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 D 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 D 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 D 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 D 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 D 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 D 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 D 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 D 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 D 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 D 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 D 316 VAL GLU VAL TYR
HET FLC A9002 13
HET FAD A 415 53
HET FLC B9001 13
HET FAD B 415 53
HET FAD C 415 53
HET FAD D 415 53
HETNAM FLC CITRATE ANION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 5 FLC 2(C6 H5 O7 3-)
FORMUL 6 FAD 4(C27 H33 N9 O15 P2)
FORMUL 11 HOH *291(H2 O)
HELIX 1 1 GLY A 136 LEU A 145 1 10
HELIX 2 2 ASP A 165 ASN A 170 1 6
HELIX 3 3 ILE A 182 PHE A 193 1 12
HELIX 4 4 ASN A 219 ILE A 223 5 5
HELIX 5 5 TYR A 225 TYR A 236 1 12
HELIX 6 6 ASN A 251 ARG A 266 1 16
HELIX 7 7 ARG A 266 ASN A 276 1 11
HELIX 8 8 SER A 288 ASP A 301 1 14
HELIX 9 9 ASP A 304 LYS A 309 1 6
HELIX 10 10 GLY B 136 LEU B 145 1 10
HELIX 11 11 ILE B 182 PHE B 193 1 12
HELIX 12 12 ASN B 219 ILE B 223 5 5
HELIX 13 13 TYR B 225 TYR B 236 1 12
HELIX 14 14 ASN B 251 ARG B 266 1 16
HELIX 15 15 ARG B 266 TYR B 277 1 12
HELIX 16 16 SER B 288 SER B 299 1 12
HELIX 17 17 LYS B 307 LYS B 309 5 3
HELIX 18 18 GLY C 136 LEU C 145 1 10
HELIX 19 19 ASP C 165 ASN C 170 1 6
HELIX 20 20 ILE C 182 PHE C 193 1 12
HELIX 21 21 ASN C 219 ILE C 223 5 5
HELIX 22 22 TYR C 225 TYR C 236 1 12
HELIX 23 23 ASN C 251 ARG C 266 1 16
HELIX 24 24 ARG C 266 ASN C 276 1 11
HELIX 25 25 SER C 288 LYS C 298 1 11
HELIX 26 26 LYS C 307 LYS C 309 5 3
HELIX 27 27 GLY D 136 LEU D 145 1 10
HELIX 28 28 ASP D 165 ASN D 170 1 6
HELIX 29 29 ILE D 182 PHE D 193 1 12
HELIX 30 30 ASN D 219 ILE D 223 5 5
HELIX 31 31 TYR D 225 TYR D 236 1 12
HELIX 32 32 ASN D 251 ARG D 266 1 16
HELIX 33 33 ARG D 266 TYR D 277 1 12
HELIX 34 34 LYS D 287 LYS D 298 1 12
HELIX 35 35 LYS D 307 LYS D 309 5 3
SHEET 1 A 6 ARG A 101 SER A 104 0
SHEET 2 A 6 THR A 53 ILE A 56 -1 N ILE A 56 O ARG A 101
SHEET 3 A 6 ASP A 150 HIS A 157 -1 O THR A 154 N GLY A 55
SHEET 4 A 6 LEU A 16 ASN A 25 -1 N LEU A 16 O LEU A 153
SHEET 5 A 6 VAL A 35 ASN A 41 -1 O HIS A 37 N ILE A 24
SHEET 6 A 6 LEU A 114 LYS A 119 -1 O LEU A 114 N ILE A 40
SHEET 1 B 2 LYS A 122 TYR A 123 0
SHEET 2 B 2 ASN A 134 TYR A 135 -1 O ASN A 134 N TYR A 123
SHEET 1 C 5 ILE A 240 PHE A 246 0
SHEET 2 C 5 ILE A 211 VAL A 217 1 N ILE A 213 O HIS A 243
SHEET 3 C 5 PHE A 173 THR A 178 1 N PHE A 175 O THR A 212
SHEET 4 C 5 GLU A 280 HIS A 286 1 O TYR A 282 N ILE A 176
SHEET 5 C 5 VAL A 311 TYR A 316 1 O HIS A 312 N LEU A 281
SHEET 1 D 6 ARG B 101 SER B 104 0
SHEET 2 D 6 THR B 53 ILE B 56 -1 N ILE B 56 O ARG B 101
SHEET 3 D 6 ASP B 150 HIS B 157 -1 O HIS B 157 N THR B 53
SHEET 4 D 6 LEU B 16 ASN B 25 -1 N LEU B 16 O LEU B 153
SHEET 5 D 6 VAL B 35 ASN B 41 -1 O HIS B 37 N ILE B 24
SHEET 6 D 6 LEU B 114 LYS B 119 -1 O LEU B 114 N ILE B 40
SHEET 1 E 2 LYS B 122 TYR B 123 0
SHEET 2 E 2 ASN B 134 TYR B 135 -1 O ASN B 134 N TYR B 123
SHEET 1 F 5 ILE B 240 PHE B 246 0
SHEET 2 F 5 ILE B 211 VAL B 217 1 N ILE B 213 O HIS B 243
SHEET 3 F 5 PHE B 173 THR B 178 1 N PHE B 175 O THR B 212
SHEET 4 F 5 GLU B 280 HIS B 286 1 O TYR B 282 N ILE B 174
SHEET 5 F 5 VAL B 311 TYR B 316 1 O HIS B 312 N LEU B 281
SHEET 1 G 6 ARG C 101 SER C 104 0
SHEET 2 G 6 THR C 53 ILE C 56 -1 N ILE C 56 O ARG C 101
SHEET 3 G 6 ASP C 150 HIS C 157 -1 O HIS C 157 N THR C 53
SHEET 4 G 6 LEU C 16 ASN C 25 -1 N CYS C 18 O ILE C 151
SHEET 5 G 6 VAL C 35 ASN C 41 -1 O HIS C 37 N ILE C 24
SHEET 6 G 6 LEU C 114 LYS C 119 -1 O LEU C 114 N ILE C 40
SHEET 1 H 5 ILE C 240 PHE C 246 0
SHEET 2 H 5 ILE C 211 VAL C 217 1 N ILE C 213 O HIS C 243
SHEET 3 H 5 PHE C 173 THR C 178 1 N PHE C 175 O THR C 212
SHEET 4 H 5 GLU C 280 HIS C 286 1 O TYR C 282 N ILE C 174
SHEET 5 H 5 VAL C 311 TYR C 316 1 O HIS C 312 N LEU C 281
SHEET 1 I 6 ARG D 101 SER D 104 0
SHEET 2 I 6 THR D 53 ILE D 56 -1 N ILE D 56 O ARG D 101
SHEET 3 I 6 ASP D 150 HIS D 157 -1 O THR D 154 N GLY D 55
SHEET 4 I 6 LEU D 16 ASN D 25 -1 N CYS D 18 O ILE D 151
SHEET 5 I 6 VAL D 35 ASN D 41 -1 O HIS D 37 N ILE D 24
SHEET 6 I 6 LEU D 114 LYS D 119 -1 O LEU D 114 N ILE D 40
SHEET 1 J 5 ILE D 240 PHE D 246 0
SHEET 2 J 5 ILE D 211 VAL D 217 1 N ILE D 213 O HIS D 243
SHEET 3 J 5 PHE D 173 THR D 178 1 N PHE D 175 O TYR D 214
SHEET 4 J 5 GLU D 280 HIS D 286 1 O GLU D 280 N ILE D 174
SHEET 5 J 5 VAL D 311 TYR D 316 1 O HIS D 312 N LEU D 281
SSBOND 1 CYS A 99 CYS B 99 1555 1555 2.06
SSBOND 2 CYS C 99 CYS D 99 1555 1555 2.08
CISPEP 1 GLY A 155 ALA A 156 0 12.38
CISPEP 2 GLY D 155 ALA D 156 0 2.90
SITE 1 AC1 14 LYS A 267 HIS A 300 TYR B 218 TYR B 248
SITE 2 AC1 14 LYS B 249 GLN B 250 HOH B9022 HOH B9066
SITE 3 AC1 14 HOH B9070 HOH B9075 HOH B9077 PHE C 257
SITE 4 AC1 14 TYR C 258 TYR D 264
SITE 1 AC2 9 ASN A 275 ASN A 276 LYS A 278 GLU B 220
SITE 2 AC2 9 LEU B 226 GLU B 230 TYR B 244 PHE B 246
SITE 3 AC2 9 HOH B9044
SITE 1 AC3 21 ARG A 101 LEU A 102 TYR A 103 SER A 104
SITE 2 AC3 21 ALA A 117 ILE A 118 LYS A 119 HIS A 121
SITE 3 AC3 21 TYR A 123 GLY A 136 TYR A 137 CYS A 138
SITE 4 AC3 21 SER A 139 THR A 180 TYR A 316 HOH A9006
SITE 5 AC3 21 HOH A9008 HOH A9013 HOH A9018 HOH A9029
SITE 6 AC3 21 LYS B 13
SITE 1 AC4 24 LYS A 13 ARG B 101 LEU B 102 TYR B 103
SITE 2 AC4 24 SER B 104 ALA B 117 ILE B 118 LYS B 119
SITE 3 AC4 24 HIS B 121 TYR B 123 GLY B 136 TYR B 137
SITE 4 AC4 24 CYS B 138 SER B 139 THR B 180 GLU B 314
SITE 5 AC4 24 TYR B 316 HOH B9003 HOH B9004 HOH B9008
SITE 6 AC4 24 HOH B9011 HOH B9034 HOH B9038 HOH B9080
SITE 1 AC5 23 THR C 53 ARG C 101 LEU C 102 TYR C 103
SITE 2 AC5 23 SER C 104 ALA C 117 ILE C 118 LYS C 119
SITE 3 AC5 23 HIS C 121 TYR C 123 GLY C 136 TYR C 137
SITE 4 AC5 23 CYS C 138 SER C 139 THR C 180 TYR C 316
SITE 5 AC5 23 HOH C 416 HOH C 417 HOH C 419 HOH C 428
SITE 6 AC5 23 HOH C 432 HOH C 470 LYS D 13
SITE 1 AC6 20 LYS C 13 ARG D 101 LEU D 102 TYR D 103
SITE 2 AC6 20 SER D 104 ALA D 117 ILE D 118 LYS D 119
SITE 3 AC6 20 HIS D 121 TYR D 123 GLY D 136 TYR D 137
SITE 4 AC6 20 CYS D 138 SER D 139 THR D 180 TYR D 316
SITE 5 AC6 20 HOH D 416 HOH D 417 HOH D 420 HOH D 421
CRYST1 138.038 138.038 147.362 90.00 90.00 120.00 P 32 2 1 24
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 0.007244 0.004183 0.000000 0.00000
SCALE2 0.000000 0.008365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
