HEADER OXIDOREDUCTASE 13-JAN-05 1YJ8
TITLE INITIAL STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM GLYCEROL-3-
TITLE 2 PHOSPHATE DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 1.1.1.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 GENE: PFL0780W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21STAR/DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 SYSTEM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS SGPP, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA CONSORTIUM,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ROBIEN,W.G.J.HOL,STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA
AUTHOR 2 CONSORTIUM (SGPP)
REVDAT 3 13-JUL-11 1YJ8 1 VERSN
REVDAT 2 24-FEB-09 1YJ8 1 VERSN
REVDAT 1 01-FEB-05 1YJ8 0
JRNL AUTH M.A.ROBIEN,W.G.J.HOL,
JRNL AUTH 2 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA (SGPP)
JRNL TITL INITIAL STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM
JRNL TITL 2 GLYCEROL-3-PHOSPHATE DEHYDROGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 47958
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2557
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6604
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE SET COUNT : 364
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8415
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : -0.01000
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): 0.528
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.312
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.246
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.568
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8565 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7825 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11560 ; 0.944 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18299 ; 0.730 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1062 ; 4.761 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 374 ;39.426 ;25.749
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1578 ;14.926 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;14.453 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1331 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9374 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1623 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1790 ; 0.188 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7865 ; 0.158 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4203 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4739 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 182 ; 0.127 ; 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): 30 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 107 ; 0.221 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.090 ; 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): 5720 ; 1.011 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2172 ; 0.113 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8606 ; 1.694 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3541 ; 1.406 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2954 ; 2.229 ;10.000
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 28 3
REMARK 3 1 B 10 B 28 3
REMARK 3 1 C 10 C 28 3
REMARK 3 2 A 31 A 62 3
REMARK 3 2 B 31 B 62 3
REMARK 3 2 C 31 C 62 3
REMARK 3 3 A 66 A 88 3
REMARK 3 3 B 66 B 88 3
REMARK 3 3 C 66 C 88 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 436 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 436 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 436 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 746 ; 0.59 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 746 ; 0.62 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 746 ; 0.63 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 436 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 436 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 436 ; 0.04 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 746 ; 0.82 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 746 ; 1.03 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 746 ; 1.18 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 113 A 124 3
REMARK 3 1 B 113 B 124 3
REMARK 3 1 C 113 C 124 3
REMARK 3 2 A 129 A 210 3
REMARK 3 2 B 129 B 210 3
REMARK 3 2 C 129 C 210 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 558 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 558 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 558 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 A (A): 822 ; 0.50 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 B (A): 822 ; 0.46 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 C (A): 822 ; 0.46 ; 5.00
REMARK 3 TIGHT THERMAL 2 A (A**2): 558 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 558 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 558 ; 0.03 ; 0.50
REMARK 3 LOOSE THERMAL 2 A (A**2): 822 ; 1.18 ; 10.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 822 ; 1.14 ; 10.00
REMARK 3 LOOSE THERMAL 2 C (A**2): 822 ; 1.22 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 216 A 285 3
REMARK 3 1 B 216 B 285 3
REMARK 3 1 C 216 C 285 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 413 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 B (A): 413 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 C (A): 413 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 3 A (A): 624 ; 0.58 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 B (A): 624 ; 0.60 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 C (A): 624 ; 0.50 ; 5.00
REMARK 3 TIGHT THERMAL 3 A (A**2): 413 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 3 B (A**2): 413 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 3 C (A**2): 413 ; 0.04 ; 0.50
REMARK 3 LOOSE THERMAL 3 A (A**2): 624 ; 1.53 ; 10.00
REMARK 3 LOOSE THERMAL 3 B (A**2): 624 ; 0.89 ; 10.00
REMARK 3 LOOSE THERMAL 3 C (A**2): 624 ; 1.41 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 312 A 320 3
REMARK 3 1 B 312 B 320 3
REMARK 3 1 C 312 C 320 3
REMARK 3 2 A 323 A 372 3
REMARK 3 2 B 323 B 372 3
REMARK 3 2 C 323 C 372 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 351 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 B (A): 351 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 C (A): 351 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 4 A (A): 576 ; 0.72 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 B (A): 576 ; 0.61 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 C (A): 576 ; 0.69 ; 5.00
REMARK 3 TIGHT THERMAL 4 A (A**2): 351 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 4 B (A**2): 351 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 4 C (A**2): 351 ; 0.05 ; 0.50
REMARK 3 LOOSE THERMAL 4 A (A**2): 576 ; 1.42 ; 10.00
REMARK 3 LOOSE THERMAL 4 B (A**2): 576 ; 0.96 ; 10.00
REMARK 3 LOOSE THERMAL 4 C (A**2): 576 ; 1.56 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE AUTHORS
REMARK 3 STATE THAT THE ELECTRON DENSITY OF RESIDUES IN THE REGION OF
REMARK 3 APPROXIMATELY
REMARK 3 RESIDUES 285-313 IS QUITE WEAK, AND HENCE SOMEWHAT UNCERTAIN,
REMARK 3 ESPECIALLY IN CHAINS B AND C.
REMARK 4
REMARK 4 1YJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-05.
REMARK 100 THE RCSB ID CODE IS RCSB031576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-04; 20-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 10
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SSRL; ALS
REMARK 200 BEAMLINE : BL11-3; 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976; 0.9794, 0.91840, 0.97950
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50574
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.70800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, POTASSIUM PHOSPHATE
REMARK 280 MONOBASIC, CAPS, DTT, PH 10, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
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 116.34950
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 116.34950
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 116.34950
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 0.00000
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 0.00000
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 116.34950
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 116.34950
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 116.34950
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 88.72750
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 153.68054
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 116.34950
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: 4410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 MET A 9
REMARK 465 VAL A 63
REMARK 465 ASN A 64
REMARK 465 GLY A 65
REMARK 465 SER A 126
REMARK 465 GLU A 127
REMARK 465 SER A 128
REMARK 465 LEU A 373
REMARK 465 ASN A 374
REMARK 465 LEU A 375
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 MET B 9
REMARK 465 VAL B 63
REMARK 465 ASN B 64
REMARK 465 GLY B 65
REMARK 465 SER B 126
REMARK 465 GLU B 127
REMARK 465 SER B 128
REMARK 465 LEU B 373
REMARK 465 ASN B 374
REMARK 465 LEU B 375
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 MET C 9
REMARK 465 VAL C 63
REMARK 465 ASN C 64
REMARK 465 GLY C 65
REMARK 465 SER C 126
REMARK 465 GLU C 127
REMARK 465 SER C 128
REMARK 465 LEU C 373
REMARK 465 ASN C 374
REMARK 465 LEU C 375
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 304 CE NZ
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 LYS A 316 CG CD CE NZ
REMARK 470 LYS B 130 CD CE NZ
REMARK 470 LYS B 148 CD CE NZ
REMARK 470 LYS B 304 CE NZ
REMARK 470 GLU B 313 CG CD OE1 OE2
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 470 LYS C 124 CD CE NZ
REMARK 470 LYS C 147 CD CE NZ
REMARK 470 LYS C 148 CG CD CE NZ
REMARK 470 LYS C 304 CE NZ
REMARK 470 GLU C 313 CG CD OE1 OE2
REMARK 470 LYS C 316 CG CD CE NZ
REMARK 470 GLN C 321 CB CG CD OE1 NE2
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 149 14.94 56.91
REMARK 500 GLN A 266 -12.83 69.74
REMARK 500 THR A 302 -100.91 65.74
REMARK 500 SER B 29 17.89 -143.90
REMARK 500 ASN B 149 15.89 56.09
REMARK 500 GLN B 266 -9.96 67.48
REMARK 500 ASN B 291 -55.45 -176.04
REMARK 500 LYS B 300 -56.62 -148.79
REMARK 500 ASN C 149 15.86 55.61
REMARK 500 GLN C 266 -11.51 69.33
REMARK 500 ARG C 290 39.90 -160.30
REMARK 500 SER C 301 85.28 -159.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFAL009132AAA RELATED DB: TARGETDB
DBREF 1YJ8 A 9 375 UNP Q8I5P5 Q8I5P5_PLAF7 1 367
DBREF 1YJ8 B 9 375 UNP Q8I5P5 Q8I5P5_PLAF7 1 367
DBREF 1YJ8 C 9 375 UNP Q8I5P5 Q8I5P5_PLAF7 1 367
SEQADV 1YJ8 MET A 1 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 ALA A 2 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 3 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 4 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 5 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 6 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 7 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS A 8 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 MET B 1 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 ALA B 2 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 3 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 4 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 5 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 6 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 7 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS B 8 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 MET C 1 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 ALA C 2 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 3 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 4 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 5 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 6 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 7 UNP Q8I5P5 CLONING ARTIFACT
SEQADV 1YJ8 HIS C 8 UNP Q8I5P5 CLONING ARTIFACT
SEQRES 1 A 375 MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU
SEQRES 2 A 375 PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE
SEQRES 3 A 375 LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL
SEQRES 4 A 375 VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN
SEQRES 5 A 375 GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY
SEQRES 6 A 375 GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN
SEQRES 7 A 375 THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE
SEQRES 8 A 375 VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA
SEQRES 9 A 375 ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU
SEQRES 10 A 375 SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS
SEQRES 11 A 375 ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY
SEQRES 12 A 375 PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN
SEQRES 13 A 375 TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU
SEQRES 14 A 375 SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN
SEQRES 15 A 375 PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER
SEQRES 16 A 375 LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE
SEQRES 17 A 375 LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE
SEQRES 18 A 375 CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY
SEQRES 19 A 375 PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER
SEQRES 20 A 375 ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE
SEQRES 21 A 375 GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU
SEQRES 22 A 375 LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE
SEQRES 23 A 375 LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE
SEQRES 24 A 375 LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN
SEQRES 25 A 375 GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR
SEQRES 26 A 375 LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET
SEQRES 27 A 375 THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE
SEQRES 28 A 375 SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR
SEQRES 29 A 375 PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU
SEQRES 1 B 375 MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU
SEQRES 2 B 375 PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE
SEQRES 3 B 375 LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL
SEQRES 4 B 375 VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN
SEQRES 5 B 375 GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY
SEQRES 6 B 375 GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN
SEQRES 7 B 375 THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE
SEQRES 8 B 375 VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA
SEQRES 9 B 375 ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU
SEQRES 10 B 375 SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS
SEQRES 11 B 375 ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY
SEQRES 12 B 375 PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN
SEQRES 13 B 375 TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU
SEQRES 14 B 375 SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN
SEQRES 15 B 375 PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER
SEQRES 16 B 375 LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE
SEQRES 17 B 375 LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE
SEQRES 18 B 375 CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY
SEQRES 19 B 375 PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER
SEQRES 20 B 375 ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE
SEQRES 21 B 375 GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU
SEQRES 22 B 375 LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE
SEQRES 23 B 375 LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE
SEQRES 24 B 375 LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN
SEQRES 25 B 375 GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR
SEQRES 26 B 375 LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET
SEQRES 27 B 375 THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE
SEQRES 28 B 375 SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR
SEQRES 29 B 375 PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU
SEQRES 1 C 375 MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU
SEQRES 2 C 375 PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE
SEQRES 3 C 375 LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL
SEQRES 4 C 375 VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN
SEQRES 5 C 375 GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY
SEQRES 6 C 375 GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN
SEQRES 7 C 375 THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE
SEQRES 8 C 375 VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA
SEQRES 9 C 375 ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU
SEQRES 10 C 375 SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS
SEQRES 11 C 375 ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY
SEQRES 12 C 375 PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN
SEQRES 13 C 375 TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU
SEQRES 14 C 375 SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN
SEQRES 15 C 375 PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER
SEQRES 16 C 375 LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE
SEQRES 17 C 375 LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE
SEQRES 18 C 375 CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY
SEQRES 19 C 375 PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER
SEQRES 20 C 375 ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE
SEQRES 21 C 375 GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU
SEQRES 22 C 375 LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE
SEQRES 23 C 375 LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE
SEQRES 24 C 375 LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN
SEQRES 25 C 375 GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR
SEQRES 26 C 375 LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET
SEQRES 27 C 375 THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE
SEQRES 28 C 375 SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR
SEQRES 29 C 375 PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU
FORMUL 4 HOH *10(H2 O)
HELIX 1 1 ASN A 12 GLY A 20 1 9
HELIX 2 2 GLY A 30 ASN A 47 1 18
HELIX 3 3 ARG A 67 HIS A 76 1 10
HELIX 4 4 LEU A 97 ASN A 102 1 6
HELIX 5 5 PRO A 112 LYS A 124 1 13
HELIX 6 6 LEU A 153 LEU A 162 1 10
HELIX 7 7 ILE A 174 MET A 180 1 7
HELIX 8 8 ASP A 192 ASP A 204 1 13
HELIX 9 9 THR A 216 LEU A 239 1 24
HELIX 10 10 PRO A 242 PHE A 265 1 24
HELIX 11 11 ASN A 269 GLU A 275 5 7
HELIX 12 12 GLY A 278 LEU A 287 1 10
HELIX 13 13 ARG A 290 THR A 302 1 13
HELIX 14 14 THR A 306 LYS A 316 1 11
HELIX 15 15 LEU A 320 LYS A 336 1 17
HELIX 16 16 MET A 338 GLU A 341 5 4
HELIX 17 17 PHE A 342 GLU A 354 1 13
HELIX 18 18 SER A 359 MET A 366 1 8
HELIX 19 19 ASN B 12 GLY B 20 1 9
HELIX 20 20 GLY B 30 ASN B 47 1 18
HELIX 21 21 ARG B 67 HIS B 76 1 10
HELIX 22 22 LEU B 97 ASN B 102 1 6
HELIX 23 23 PRO B 112 LYS B 124 1 13
HELIX 24 24 LEU B 153 LEU B 162 1 10
HELIX 25 25 ILE B 174 MET B 180 1 7
HELIX 26 26 ASP B 192 ASP B 204 1 13
HELIX 27 27 THR B 216 LEU B 239 1 24
HELIX 28 28 PRO B 242 PHE B 265 1 24
HELIX 29 29 ASN B 269 GLU B 275 5 7
HELIX 30 30 GLY B 278 ALA B 288 1 11
HELIX 31 31 ALA B 288 ILE B 299 1 12
HELIX 32 32 THR B 306 ILE B 314 1 9
HELIX 33 33 LEU B 320 LYS B 336 1 17
HELIX 34 34 MET B 338 GLU B 341 5 4
HELIX 35 35 PHE B 342 GLU B 354 1 13
HELIX 36 36 SER B 359 MET B 366 1 8
HELIX 37 37 ASN C 12 GLY C 20 1 9
HELIX 38 38 GLY C 30 ASN C 47 1 18
HELIX 39 39 ARG C 67 HIS C 76 1 10
HELIX 40 40 LEU C 97 ASN C 102 1 6
HELIX 41 41 PRO C 112 LYS C 124 1 13
HELIX 42 42 LEU C 153 LEU C 162 1 10
HELIX 43 43 ILE C 174 MET C 180 1 7
HELIX 44 44 ASP C 192 ASP C 204 1 13
HELIX 45 45 THR C 216 LEU C 239 1 24
HELIX 46 46 PRO C 242 PHE C 265 1 24
HELIX 47 47 ASN C 269 GLU C 275 5 7
HELIX 48 48 GLY C 278 ALA C 288 1 11
HELIX 49 49 ASN C 291 SER C 301 1 11
HELIX 50 50 THR C 306 ILE C 314 1 9
HELIX 51 51 LEU C 320 LYS C 336 1 17
HELIX 52 52 PHE C 342 GLU C 354 1 13
HELIX 53 53 SER C 359 MET C 366 1 8
SHEET 1 A 8 ILE A 91 HIS A 94 0
SHEET 2 A 8 VAL A 54 TRP A 57 1 N MET A 56 O VAL A 92
SHEET 3 A 8 ILE A 24 LEU A 27 1 N ILE A 26 O TRP A 57
SHEET 4 A 8 LEU A 106 PHE A 109 1 O ILE A 108 N SER A 25
SHEET 5 A 8 LYS A 136 SER A 139 1 O ILE A 138 N PHE A 109
SHEET 6 A 8 CYS A 166 SER A 170 1 O LEU A 169 N SER A 139
SHEET 7 A 8 SER A 184 GLY A 189 -1 O THR A 187 N SER A 170
SHEET 8 A 8 PHE A 208 VAL A 213 1 O ASN A 211 N ILE A 188
SHEET 1 B 2 ILE A 145 LYS A 147 0
SHEET 2 B 2 GLN A 150 LYS A 152 -1 O LYS A 152 N ILE A 145
SHEET 1 C 8 ILE B 91 HIS B 94 0
SHEET 2 C 8 VAL B 54 TRP B 57 1 N MET B 56 O VAL B 92
SHEET 3 C 8 ILE B 24 LEU B 27 1 N ILE B 26 O TRP B 57
SHEET 4 C 8 LEU B 106 PHE B 109 1 O ILE B 108 N SER B 25
SHEET 5 C 8 LYS B 136 SER B 139 1 O ILE B 138 N PHE B 109
SHEET 6 C 8 CYS B 166 SER B 170 1 O LEU B 169 N SER B 139
SHEET 7 C 8 SER B 184 GLY B 189 -1 O THR B 187 N SER B 170
SHEET 8 C 8 PHE B 208 VAL B 213 1 O ASN B 211 N ILE B 188
SHEET 1 D 2 ILE B 145 LYS B 147 0
SHEET 2 D 2 GLN B 150 LYS B 152 -1 O LYS B 152 N ILE B 145
SHEET 1 E 8 ILE C 91 HIS C 94 0
SHEET 2 E 8 VAL C 54 TRP C 57 1 N MET C 56 O VAL C 92
SHEET 3 E 8 ILE C 24 LEU C 27 1 N ILE C 26 O TRP C 57
SHEET 4 E 8 LEU C 106 PHE C 109 1 O ILE C 108 N SER C 25
SHEET 5 E 8 LYS C 136 SER C 139 1 O ILE C 138 N PHE C 109
SHEET 6 E 8 CYS C 166 SER C 170 1 O LEU C 169 N SER C 139
SHEET 7 E 8 SER C 184 GLY C 189 -1 O THR C 187 N SER C 170
SHEET 8 E 8 PHE C 208 VAL C 213 1 O ASN C 211 N ILE C 188
SHEET 1 F 2 ILE C 145 LYS C 147 0
SHEET 2 F 2 GLN C 150 LYS C 152 -1 O LYS C 152 N ILE C 145
CRYST1 177.455 177.455 232.699 90.00 90.00 120.00 P 63 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 0.005635 0.003254 0.000000 0.00000
SCALE2 0.000000 0.006507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
