HEADER TRANSFERASE/TRANSFERASE INHIBITOR 03-NOV-10 3PHC
TITLE CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM PURINE NUCLEOSIDE
TITLE 2 PHOSPHORYLASE IN COMPLEX WITH DADME-IMMG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE NUCLEOSIDE PHOSPHORYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 2.4.2.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 GENE: PNP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHIS2 TOPO
KEYWDS PNP, IMMUCILLIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HO,A.A.EDWARDS,S.C.ALMO,V.L.SCHRAMM
REVDAT 3 21-FEB-24 3PHC 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3PHC 1 REMARK
REVDAT 1 09-NOV-11 3PHC 0
JRNL AUTH M.HO,A.A.EDWARDS,S.C.ALMO,V.L.SCHRAMM
JRNL TITL CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM PURINE NUCLEOSIDE
JRNL TITL 2 PHOSPHORYLASE IN COMPLEX WITH DADME-IMMG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 95775
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4781
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5203
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11166
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 153
REMARK 3 SOLVENT ATOMS : 312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -3.54000
REMARK 3 B12 (A**2) : 2.35000
REMARK 3 B13 (A**2) : 1.48000
REMARK 3 B23 (A**2) : 2.21000
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): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.362
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11514 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15594 ; 1.317 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1452 ; 6.051 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 474 ;39.929 ;24.810
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2004 ;14.274 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;17.061 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1788 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8496 ; 0.005 ; 0.021
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): 7224 ; 0.559 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11652 ; 1.055 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4290 ; 1.678 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3942 ; 2.720 ; 4.500
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 : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3PHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95778
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.15200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM FORMATE, 10% PEG 3350, PH
REMARK 280 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 0
REMARK 465 LEU A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 246
REMARK 465 GLY A 247
REMARK 465 GLU A 248
REMARK 465 PHE A 249
REMARK 465 GLU A 250
REMARK 465 ALA A 251
REMARK 465 TYR A 252
REMARK 465 VAL A 253
REMARK 465 GLU A 254
REMARK 465 GLN A 255
REMARK 465 LYS A 256
REMARK 465 LEU A 257
REMARK 465 ILE A 258
REMARK 465 SER A 259
REMARK 465 GLU A 260
REMARK 465 GLU A 261
REMARK 465 ASP A 262
REMARK 465 LEU A 263
REMARK 465 ASN A 264
REMARK 465 SER A 265
REMARK 465 ALA A 266
REMARK 465 VAL A 267
REMARK 465 ASP A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 HIS A 274
REMARK 465 MET B 0
REMARK 465 LEU B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 246
REMARK 465 GLY B 247
REMARK 465 GLU B 248
REMARK 465 PHE B 249
REMARK 465 GLU B 250
REMARK 465 ALA B 251
REMARK 465 TYR B 252
REMARK 465 VAL B 253
REMARK 465 GLU B 254
REMARK 465 GLN B 255
REMARK 465 LYS B 256
REMARK 465 LEU B 257
REMARK 465 ILE B 258
REMARK 465 SER B 259
REMARK 465 GLU B 260
REMARK 465 GLU B 261
REMARK 465 ASP B 262
REMARK 465 LEU B 263
REMARK 465 ASN B 264
REMARK 465 SER B 265
REMARK 465 ALA B 266
REMARK 465 VAL B 267
REMARK 465 ASP B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 HIS B 273
REMARK 465 HIS B 274
REMARK 465 MET C 0
REMARK 465 LEU C 1
REMARK 465 ASP C 2
REMARK 465 LYS C 246
REMARK 465 GLY C 247
REMARK 465 GLU C 248
REMARK 465 PHE C 249
REMARK 465 GLU C 250
REMARK 465 ALA C 251
REMARK 465 TYR C 252
REMARK 465 VAL C 253
REMARK 465 GLU C 254
REMARK 465 GLN C 255
REMARK 465 LYS C 256
REMARK 465 LEU C 257
REMARK 465 ILE C 258
REMARK 465 SER C 259
REMARK 465 GLU C 260
REMARK 465 GLU C 261
REMARK 465 ASP C 262
REMARK 465 LEU C 263
REMARK 465 ASN C 264
REMARK 465 SER C 265
REMARK 465 ALA C 266
REMARK 465 VAL C 267
REMARK 465 ASP C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 HIS C 273
REMARK 465 HIS C 274
REMARK 465 MET D 0
REMARK 465 LEU D 1
REMARK 465 ASP D 2
REMARK 465 LYS D 246
REMARK 465 GLY D 247
REMARK 465 GLU D 248
REMARK 465 PHE D 249
REMARK 465 GLU D 250
REMARK 465 ALA D 251
REMARK 465 TYR D 252
REMARK 465 VAL D 253
REMARK 465 GLU D 254
REMARK 465 GLN D 255
REMARK 465 LYS D 256
REMARK 465 LEU D 257
REMARK 465 ILE D 258
REMARK 465 SER D 259
REMARK 465 GLU D 260
REMARK 465 GLU D 261
REMARK 465 ASP D 262
REMARK 465 LEU D 263
REMARK 465 ASN D 264
REMARK 465 SER D 265
REMARK 465 ALA D 266
REMARK 465 VAL D 267
REMARK 465 ASP D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
REMARK 465 HIS D 273
REMARK 465 HIS D 274
REMARK 465 MET E 0
REMARK 465 LEU E 1
REMARK 465 ASP E 2
REMARK 465 LYS E 246
REMARK 465 GLY E 247
REMARK 465 GLU E 248
REMARK 465 PHE E 249
REMARK 465 GLU E 250
REMARK 465 ALA E 251
REMARK 465 TYR E 252
REMARK 465 VAL E 253
REMARK 465 GLU E 254
REMARK 465 GLN E 255
REMARK 465 LYS E 256
REMARK 465 LEU E 257
REMARK 465 ILE E 258
REMARK 465 SER E 259
REMARK 465 GLU E 260
REMARK 465 GLU E 261
REMARK 465 ASP E 262
REMARK 465 LEU E 263
REMARK 465 ASN E 264
REMARK 465 SER E 265
REMARK 465 ALA E 266
REMARK 465 VAL E 267
REMARK 465 ASP E 268
REMARK 465 HIS E 269
REMARK 465 HIS E 270
REMARK 465 HIS E 271
REMARK 465 HIS E 272
REMARK 465 HIS E 273
REMARK 465 HIS E 274
REMARK 465 MET F 0
REMARK 465 LEU F 1
REMARK 465 ASP F 2
REMARK 465 LYS F 246
REMARK 465 GLY F 247
REMARK 465 GLU F 248
REMARK 465 PHE F 249
REMARK 465 GLU F 250
REMARK 465 ALA F 251
REMARK 465 TYR F 252
REMARK 465 VAL F 253
REMARK 465 GLU F 254
REMARK 465 GLN F 255
REMARK 465 LYS F 256
REMARK 465 LEU F 257
REMARK 465 ILE F 258
REMARK 465 SER F 259
REMARK 465 GLU F 260
REMARK 465 GLU F 261
REMARK 465 ASP F 262
REMARK 465 LEU F 263
REMARK 465 ASN F 264
REMARK 465 SER F 265
REMARK 465 ALA F 266
REMARK 465 VAL F 267
REMARK 465 ASP F 268
REMARK 465 HIS F 269
REMARK 465 HIS F 270
REMARK 465 HIS F 271
REMARK 465 HIS F 272
REMARK 465 HIS F 273
REMARK 465 HIS F 274
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 ARG A 45 -134.64 50.65
REMARK 500 GLU A 114 46.32 -91.65
REMARK 500 ASP A 115 -164.26 -115.09
REMARK 500 GLU A 182 -152.03 -145.31
REMARK 500 ASP A 218 112.86 -161.02
REMARK 500 ARG B 45 -129.84 57.78
REMARK 500 ARG B 102 135.71 -39.78
REMARK 500 GLU B 114 43.63 -89.08
REMARK 500 ASP B 115 -166.51 -110.70
REMARK 500 GLU B 182 -145.49 -142.58
REMARK 500 ARG C 45 -132.02 50.69
REMARK 500 GLU C 114 50.21 -91.93
REMARK 500 ASP C 115 -164.90 -118.65
REMARK 500 GLU C 182 -151.92 -143.52
REMARK 500 ARG D 45 -128.96 50.73
REMARK 500 GLU D 114 49.26 -92.57
REMARK 500 ASP D 115 -163.73 -118.32
REMARK 500 GLU D 182 -151.39 -143.84
REMARK 500 ARG E 45 -130.56 47.39
REMARK 500 GLU E 114 45.67 -91.11
REMARK 500 ASP E 115 -165.15 -111.54
REMARK 500 ILE E 165 -60.01 -101.80
REMARK 500 ASN E 177 14.45 81.03
REMARK 500 GLU E 182 -148.88 -139.55
REMARK 500 ASP E 218 115.06 -161.03
REMARK 500 SER F 37 -179.05 -172.85
REMARK 500 ARG F 45 -127.12 50.54
REMARK 500 GLU F 114 48.06 -90.40
REMARK 500 ASP F 115 -166.20 -115.66
REMARK 500 ASN F 177 16.00 81.39
REMARK 500 GLU F 182 -146.80 -139.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 275 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 46 OE1
REMARK 620 2 VAL A 66 O 159.9
REMARK 620 3 GLU B 46 OE1 80.4 91.7
REMARK 620 4 VAL B 66 O 92.5 100.6 159.8
REMARK 620 5 HOH B 304 O 111.2 88.2 99.8 65.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 275 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 46 OE1
REMARK 620 2 VAL C 66 O 158.5
REMARK 620 3 GLU D 46 OE1 87.4 88.6
REMARK 620 4 VAL D 66 O 88.2 101.8 161.4
REMARK 620 5 HOH D 291 O 112.2 89.3 97.2 68.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 275 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 46 OE1
REMARK 620 2 VAL E 66 O 161.2
REMARK 620 3 HOH E 293 O 102.6 64.9
REMARK 620 4 GLU F 46 OE1 82.3 89.9 113.3
REMARK 620 5 VAL F 66 O 93.2 99.7 87.1 159.6
REMARK 620 6 HOH F 292 O 107.5 90.7 136.6 101.2 61.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM5 F 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PHB RELATED DB: PDB
DBREF 3PHC A 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
DBREF 3PHC B 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
DBREF 3PHC C 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
DBREF 3PHC D 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
DBREF 3PHC E 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
DBREF 3PHC F 0 245 UNP Q8T9Z7 Q8T9Z7_PLAFA 1 245
SEQADV 3PHC LEU A 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS A 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY A 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU A 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE A 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU A 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA A 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR A 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL A 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU A 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN A 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS A 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU A 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE A 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER A 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU A 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU A 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP A 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU A 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN A 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER A 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA A 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL A 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP A 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS A 274 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU B 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS B 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY B 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU B 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE B 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU B 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA B 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR B 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL B 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU B 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN B 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS B 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU B 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE B 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER B 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU B 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU B 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP B 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU B 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN B 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER B 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA B 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL B 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP B 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS B 274 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU C 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS C 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY C 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU C 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE C 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU C 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA C 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR C 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL C 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU C 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN C 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS C 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU C 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE C 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER C 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU C 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU C 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP C 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU C 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN C 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER C 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA C 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL C 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP C 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS C 274 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU D 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS D 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY D 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU D 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE D 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU D 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA D 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR D 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL D 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU D 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN D 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS D 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU D 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE D 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER D 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU D 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU D 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP D 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU D 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN D 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER D 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA D 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL D 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP D 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS D 274 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU E 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS E 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY E 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU E 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE E 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU E 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA E 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR E 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL E 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU E 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN E 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS E 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU E 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE E 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER E 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU E 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU E 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP E 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU E 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN E 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER E 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA E 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL E 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP E 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS E 274 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU F 1 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS F 246 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLY F 247 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU F 248 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC PHE F 249 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU F 250 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA F 251 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC TYR F 252 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL F 253 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU F 254 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLN F 255 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LYS F 256 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU F 257 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ILE F 258 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER F 259 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU F 260 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC GLU F 261 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP F 262 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC LEU F 263 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASN F 264 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC SER F 265 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ALA F 266 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC VAL F 267 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC ASP F 268 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 269 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 270 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 271 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 272 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 273 UNP Q8T9Z7 EXPRESSION TAG
SEQADV 3PHC HIS F 274 UNP Q8T9Z7 EXPRESSION TAG
SEQRES 1 A 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 A 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 A 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 A 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 A 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 A 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 A 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 A 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 A 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 A 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 A 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 A 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 A 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 A 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 A 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 A 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 A 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 A 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 A 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 A 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 A 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 A 275 HIS HIS
SEQRES 1 B 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 B 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 B 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 B 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 B 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 B 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 B 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 B 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 B 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 B 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 B 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 B 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 B 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 B 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 B 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 B 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 B 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 B 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 B 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 B 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 B 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 B 275 HIS HIS
SEQRES 1 C 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 C 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 C 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 C 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 C 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 C 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 C 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 C 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 C 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 C 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 C 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 C 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 C 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 C 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 C 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 C 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 C 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 C 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 C 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 C 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 C 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 C 275 HIS HIS
SEQRES 1 D 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 D 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 D 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 D 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 D 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 D 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 D 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 D 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 D 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 D 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 D 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 D 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 D 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 D 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 D 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 D 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 D 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 D 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 D 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 D 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 D 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 D 275 HIS HIS
SEQRES 1 E 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 E 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 E 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 E 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 E 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 E 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 E 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 E 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 E 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 E 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 E 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 E 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 E 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 E 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 E 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 E 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 E 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 E 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 E 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 E 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 E 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 E 275 HIS HIS
SEQRES 1 F 275 MET LEU ASP ASN LEU LEU ARG HIS LEU LYS ILE SER LYS
SEQRES 2 F 275 GLU GLN ILE THR PRO VAL VAL LEU VAL VAL GLY ASP PRO
SEQRES 3 F 275 GLY ARG VAL ASP LYS ILE LYS VAL VAL CYS ASP SER TYR
SEQRES 4 F 275 VAL ASP LEU ALA TYR ASN ARG GLU TYR LYS SER VAL GLU
SEQRES 5 F 275 CYS HIS TYR LYS GLY GLN LYS PHE LEU CYS VAL SER HIS
SEQRES 6 F 275 GLY VAL GLY SER ALA GLY CYS ALA VAL CYS PHE GLU GLU
SEQRES 7 F 275 LEU CYS GLN ASN GLY ALA LYS VAL ILE ILE ARG ALA GLY
SEQRES 8 F 275 SER CYS GLY SER LEU GLN PRO ASP LEU ILE LYS ARG GLY
SEQRES 9 F 275 ASP ILE CYS ILE CYS ASN ALA ALA VAL ARG GLU ASP ARG
SEQRES 10 F 275 VAL SER HIS LEU LEU ILE HIS GLY ASP PHE PRO ALA VAL
SEQRES 11 F 275 GLY ASP PHE ASP VAL TYR ASP THR LEU ASN LYS CYS ALA
SEQRES 12 F 275 GLN GLU LEU ASN VAL PRO VAL PHE ASN GLY ILE SER VAL
SEQRES 13 F 275 SER SER ASP MET TYR TYR PRO ASN LYS ILE ILE PRO SER
SEQRES 14 F 275 ARG LEU GLU ASP TYR SER LYS ALA ASN ALA ALA VAL VAL
SEQRES 15 F 275 GLU MET GLU LEU ALA THR LEU MET VAL ILE GLY THR LEU
SEQRES 16 F 275 ARG LYS VAL LYS THR GLY GLY ILE LEU ILE VAL ASP GLY
SEQRES 17 F 275 CYS PRO PHE LYS TRP ASP GLU GLY ASP PHE ASP ASN ASN
SEQRES 18 F 275 LEU VAL PRO HIS GLN LEU GLU ASN MET ILE LYS ILE ALA
SEQRES 19 F 275 LEU GLY ALA CYS ALA LYS LEU ALA THR LYS TYR ALA LYS
SEQRES 20 F 275 GLY GLU PHE GLU ALA TYR VAL GLU GLN LYS LEU ILE SER
SEQRES 21 F 275 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 22 F 275 HIS HIS
HET K A 275 1
HET PO4 A 502 5
HET IM5 A 501 20
HET PO4 B 502 5
HET IM5 B 501 20
HET K C 275 1
HET PO4 C 502 5
HET IM5 C 501 20
HET PO4 D 502 5
HET IM5 D 501 20
HET K E 275 1
HET PO4 E 502 5
HET IM5 E 501 20
HET PO4 F 502 5
HET IM5 F 501 20
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM IM5 2-AMINO-7-{[(3R,4R)-3-HYDROXY-4-(HYDROXYMETHYL)
HETNAM 2 IM5 PYRROLIDIN-1-YL]METHYL}-3,5-DIHYDRO-4H-PYRROLO[3,2-
HETNAM 3 IM5 D]PYRIMIDIN-4-ONE
HETSYN IM5 DADME-IMMG
FORMUL 7 K 3(K 1+)
FORMUL 8 PO4 6(O4 P 3-)
FORMUL 9 IM5 6(C12 H17 N5 O3)
FORMUL 22 HOH *312(H2 O)
HELIX 1 1 SER A 11 ILE A 15 5 5
HELIX 2 2 ASP A 24 VAL A 33 1 10
HELIX 3 3 GLY A 67 GLN A 80 1 14
HELIX 4 4 ARG A 116 ILE A 122 1 7
HELIX 5 5 ASP A 131 LEU A 145 1 15
HELIX 6 6 ARG A 169 ALA A 176 1 8
HELIX 7 7 GLU A 184 ARG A 195 1 12
HELIX 8 8 CYS A 208 GLY A 215 5 8
HELIX 9 9 VAL A 222 ALA A 245 1 24
HELIX 10 10 SER B 11 ILE B 15 5 5
HELIX 11 11 ASP B 24 CYS B 35 1 12
HELIX 12 12 GLY B 67 GLN B 80 1 14
HELIX 13 13 ARG B 116 ILE B 122 1 7
HELIX 14 14 ASP B 131 LEU B 145 1 15
HELIX 15 15 ARG B 169 ALA B 176 1 8
HELIX 16 16 GLU B 184 ARG B 195 1 12
HELIX 17 17 CYS B 208 GLY B 215 5 8
HELIX 18 18 VAL B 222 THR B 242 1 21
HELIX 19 19 SER C 11 ILE C 15 5 5
HELIX 20 20 ASP C 24 VAL C 33 1 10
HELIX 21 21 GLY C 67 GLN C 80 1 14
HELIX 22 22 ARG C 116 ILE C 122 1 7
HELIX 23 23 ASP C 131 LEU C 145 1 15
HELIX 24 24 ARG C 169 ALA C 176 1 8
HELIX 25 25 GLU C 184 LYS C 196 1 13
HELIX 26 26 CYS C 208 GLY C 215 5 8
HELIX 27 27 VAL C 222 LYS C 243 1 22
HELIX 28 28 SER D 11 ILE D 15 5 5
HELIX 29 29 ASP D 24 VAL D 33 1 10
HELIX 30 30 GLY D 67 GLN D 80 1 14
HELIX 31 31 ARG D 116 ILE D 122 1 7
HELIX 32 32 ASP D 131 LEU D 145 1 15
HELIX 33 33 ARG D 169 ALA D 176 1 8
HELIX 34 34 GLU D 184 ARG D 195 1 12
HELIX 35 35 CYS D 208 GLY D 215 5 8
HELIX 36 36 VAL D 222 LYS D 243 1 22
HELIX 37 37 SER E 11 ILE E 15 5 5
HELIX 38 38 ASP E 24 VAL E 33 1 10
HELIX 39 39 GLY E 67 GLN E 80 1 14
HELIX 40 40 ARG E 116 ILE E 122 1 7
HELIX 41 41 ASP E 131 LEU E 145 1 15
HELIX 42 42 ARG E 169 ALA E 176 1 8
HELIX 43 43 GLU E 184 LYS E 196 1 13
HELIX 44 44 LYS E 211 GLY E 215 5 5
HELIX 45 45 VAL E 222 THR E 242 1 21
HELIX 46 46 SER F 11 ILE F 15 5 5
HELIX 47 47 ASP F 24 VAL F 33 1 10
HELIX 48 48 GLY F 67 GLN F 80 1 14
HELIX 49 49 ARG F 116 ILE F 122 1 7
HELIX 50 50 ASP F 131 LEU F 145 1 15
HELIX 51 51 ARG F 169 ALA F 176 1 8
HELIX 52 52 GLU F 184 LYS F 196 1 13
HELIX 53 53 CYS F 208 GLY F 215 5 8
HELIX 54 54 VAL F 222 THR F 242 1 21
SHEET 1 A 9 SER A 37 ASN A 44 0
SHEET 2 A 9 TYR A 47 TYR A 54 -1 O GLU A 51 N VAL A 39
SHEET 3 A 9 GLN A 57 SER A 63 -1 O PHE A 59 N CYS A 52
SHEET 4 A 9 VAL A 18 VAL A 22 1 N LEU A 20 O LEU A 60
SHEET 5 A 9 VAL A 85 SER A 94 1 O VAL A 85 N VAL A 19
SHEET 6 A 9 VAL A 180 GLU A 182 -1 O VAL A 181 N GLY A 93
SHEET 7 A 9 PHE A 150 SER A 157 1 N VAL A 155 O VAL A 180
SHEET 8 A 9 ILE A 105 GLU A 114 1 N ILE A 105 O PHE A 150
SHEET 9 A 9 ALA A 128 VAL A 129 -1 O ALA A 128 N ALA A 111
SHEET 1 B 8 SER A 37 ASN A 44 0
SHEET 2 B 8 TYR A 47 TYR A 54 -1 O GLU A 51 N VAL A 39
SHEET 3 B 8 GLN A 57 SER A 63 -1 O PHE A 59 N CYS A 52
SHEET 4 B 8 VAL A 18 VAL A 22 1 N LEU A 20 O LEU A 60
SHEET 5 B 8 VAL A 85 SER A 94 1 O VAL A 85 N VAL A 19
SHEET 6 B 8 LYS A 198 GLY A 207 1 O ASP A 206 N CYS A 92
SHEET 7 B 8 ILE A 105 GLU A 114 -1 N CYS A 106 O LEU A 203
SHEET 8 B 8 ALA A 128 VAL A 129 -1 O ALA A 128 N ALA A 111
SHEET 1 C 9 SER B 37 ASN B 44 0
SHEET 2 C 9 TYR B 47 TYR B 54 -1 O GLU B 51 N VAL B 39
SHEET 3 C 9 GLN B 57 SER B 63 -1 O PHE B 59 N CYS B 52
SHEET 4 C 9 VAL B 18 VAL B 22 1 N LEU B 20 O LEU B 60
SHEET 5 C 9 VAL B 85 SER B 94 1 O ILE B 87 N VAL B 21
SHEET 6 C 9 VAL B 180 GLU B 182 -1 O VAL B 181 N GLY B 93
SHEET 7 C 9 PHE B 150 SER B 157 1 N VAL B 155 O VAL B 180
SHEET 8 C 9 ILE B 105 GLU B 114 1 N ILE B 107 O PHE B 150
SHEET 9 C 9 ALA B 128 VAL B 129 -1 O ALA B 128 N ALA B 111
SHEET 1 D 8 SER B 37 ASN B 44 0
SHEET 2 D 8 TYR B 47 TYR B 54 -1 O GLU B 51 N VAL B 39
SHEET 3 D 8 GLN B 57 SER B 63 -1 O PHE B 59 N CYS B 52
SHEET 4 D 8 VAL B 18 VAL B 22 1 N LEU B 20 O LEU B 60
SHEET 5 D 8 VAL B 85 SER B 94 1 O ILE B 87 N VAL B 21
SHEET 6 D 8 LYS B 198 VAL B 205 1 O LYS B 198 N ILE B 86
SHEET 7 D 8 ILE B 105 GLU B 114 -1 N CYS B 106 O LEU B 203
SHEET 8 D 8 ALA B 128 VAL B 129 -1 O ALA B 128 N ALA B 111
SHEET 1 E 9 SER C 37 ASN C 44 0
SHEET 2 E 9 TYR C 47 TYR C 54 -1 O GLU C 51 N VAL C 39
SHEET 3 E 9 GLN C 57 SER C 63 -1 O PHE C 59 N CYS C 52
SHEET 4 E 9 VAL C 18 VAL C 22 1 N LEU C 20 O LEU C 60
SHEET 5 E 9 VAL C 85 SER C 94 1 O ILE C 87 N VAL C 21
SHEET 6 E 9 VAL C 180 GLU C 182 -1 O VAL C 181 N GLY C 93
SHEET 7 E 9 PHE C 150 SER C 157 1 N VAL C 155 O VAL C 180
SHEET 8 E 9 ILE C 105 GLU C 114 1 N ILE C 107 O PHE C 150
SHEET 9 E 9 ALA C 128 VAL C 129 -1 O ALA C 128 N ALA C 111
SHEET 1 F 8 SER C 37 ASN C 44 0
SHEET 2 F 8 TYR C 47 TYR C 54 -1 O GLU C 51 N VAL C 39
SHEET 3 F 8 GLN C 57 SER C 63 -1 O PHE C 59 N CYS C 52
SHEET 4 F 8 VAL C 18 VAL C 22 1 N LEU C 20 O LEU C 60
SHEET 5 F 8 VAL C 85 SER C 94 1 O ILE C 87 N VAL C 21
SHEET 6 F 8 LYS C 198 VAL C 205 1 O LYS C 198 N ILE C 86
SHEET 7 F 8 ILE C 105 GLU C 114 -1 N CYS C 106 O LEU C 203
SHEET 8 F 8 ALA C 128 VAL C 129 -1 O ALA C 128 N ALA C 111
SHEET 1 G 9 SER D 37 ASN D 44 0
SHEET 2 G 9 TYR D 47 TYR D 54 -1 O GLU D 51 N VAL D 39
SHEET 3 G 9 GLN D 57 SER D 63 -1 O PHE D 59 N CYS D 52
SHEET 4 G 9 VAL D 18 VAL D 22 1 N LEU D 20 O LEU D 60
SHEET 5 G 9 VAL D 85 SER D 94 1 O ALA D 89 N VAL D 21
SHEET 6 G 9 VAL D 180 GLU D 182 -1 O VAL D 181 N GLY D 93
SHEET 7 G 9 PHE D 150 SER D 157 1 N VAL D 155 O VAL D 180
SHEET 8 G 9 ILE D 105 GLU D 114 1 N ILE D 107 O PHE D 150
SHEET 9 G 9 ALA D 128 VAL D 129 -1 O ALA D 128 N ALA D 111
SHEET 1 H 8 SER D 37 ASN D 44 0
SHEET 2 H 8 TYR D 47 TYR D 54 -1 O GLU D 51 N VAL D 39
SHEET 3 H 8 GLN D 57 SER D 63 -1 O PHE D 59 N CYS D 52
SHEET 4 H 8 VAL D 18 VAL D 22 1 N LEU D 20 O LEU D 60
SHEET 5 H 8 VAL D 85 SER D 94 1 O ALA D 89 N VAL D 21
SHEET 6 H 8 LYS D 198 VAL D 205 1 O ILE D 202 N ARG D 88
SHEET 7 H 8 ILE D 105 GLU D 114 -1 N CYS D 106 O LEU D 203
SHEET 8 H 8 ALA D 128 VAL D 129 -1 O ALA D 128 N ALA D 111
SHEET 1 I 9 SER E 37 ASN E 44 0
SHEET 2 I 9 TYR E 47 TYR E 54 -1 O GLU E 51 N VAL E 39
SHEET 3 I 9 GLN E 57 SER E 63 -1 O PHE E 59 N CYS E 52
SHEET 4 I 9 VAL E 18 VAL E 22 1 N LEU E 20 O LEU E 60
SHEET 5 I 9 VAL E 85 SER E 94 1 O ILE E 87 N VAL E 21
SHEET 6 I 9 VAL E 180 GLU E 182 -1 O VAL E 181 N GLY E 93
SHEET 7 I 9 PHE E 150 SER E 157 1 N VAL E 155 O VAL E 180
SHEET 8 I 9 ILE E 105 GLU E 114 1 N ILE E 107 O PHE E 150
SHEET 9 I 9 ALA E 128 VAL E 129 -1 O ALA E 128 N ALA E 111
SHEET 1 J 8 SER E 37 ASN E 44 0
SHEET 2 J 8 TYR E 47 TYR E 54 -1 O GLU E 51 N VAL E 39
SHEET 3 J 8 GLN E 57 SER E 63 -1 O PHE E 59 N CYS E 52
SHEET 4 J 8 VAL E 18 VAL E 22 1 N LEU E 20 O LEU E 60
SHEET 5 J 8 VAL E 85 SER E 94 1 O ILE E 87 N VAL E 21
SHEET 6 J 8 LYS E 198 VAL E 205 1 O ILE E 202 N ARG E 88
SHEET 7 J 8 ILE E 105 GLU E 114 -1 N CYS E 106 O LEU E 203
SHEET 8 J 8 ALA E 128 VAL E 129 -1 O ALA E 128 N ALA E 111
SHEET 1 K 9 SER F 37 ASN F 44 0
SHEET 2 K 9 TYR F 47 TYR F 54 -1 O GLU F 51 N VAL F 39
SHEET 3 K 9 GLN F 57 SER F 63 -1 O PHE F 59 N CYS F 52
SHEET 4 K 9 VAL F 18 VAL F 22 1 N LEU F 20 O LEU F 60
SHEET 5 K 9 VAL F 85 SER F 94 1 O ILE F 87 N VAL F 21
SHEET 6 K 9 VAL F 180 GLU F 182 -1 O VAL F 181 N GLY F 93
SHEET 7 K 9 PHE F 150 SER F 157 1 N VAL F 155 O VAL F 180
SHEET 8 K 9 ILE F 105 GLU F 114 1 N ILE F 107 O PHE F 150
SHEET 9 K 9 ALA F 128 VAL F 129 -1 O ALA F 128 N ALA F 111
SHEET 1 L 8 SER F 37 ASN F 44 0
SHEET 2 L 8 TYR F 47 TYR F 54 -1 O GLU F 51 N VAL F 39
SHEET 3 L 8 GLN F 57 SER F 63 -1 O PHE F 59 N CYS F 52
SHEET 4 L 8 VAL F 18 VAL F 22 1 N LEU F 20 O LEU F 60
SHEET 5 L 8 VAL F 85 SER F 94 1 O ILE F 87 N VAL F 21
SHEET 6 L 8 LYS F 198 GLY F 207 1 O ASP F 206 N CYS F 92
SHEET 7 L 8 ILE F 105 GLU F 114 -1 N CYS F 106 O LEU F 203
SHEET 8 L 8 ALA F 128 VAL F 129 -1 O ALA F 128 N ALA F 111
LINK OE1 GLU A 46 K K A 275 1555 1555 2.73
LINK O VAL A 66 K K A 275 1555 1555 2.86
LINK K K A 275 OE1 GLU B 46 1555 1555 2.71
LINK K K A 275 O VAL B 66 1555 1555 2.81
LINK K K A 275 O HOH B 304 1555 1555 3.12
LINK OE1 GLU C 46 K K C 275 1555 1555 2.70
LINK O VAL C 66 K K C 275 1555 1555 2.82
LINK K K C 275 OE1 GLU D 46 1555 1555 2.84
LINK K K C 275 O VAL D 66 1555 1555 2.83
LINK K K C 275 O HOH D 291 1555 1555 2.91
LINK OE1 GLU E 46 K K E 275 1555 1555 2.73
LINK O VAL E 66 K K E 275 1555 1555 2.74
LINK K K E 275 O HOH E 293 1555 1555 2.71
LINK K K E 275 OE1 GLU F 46 1555 1555 2.73
LINK K K E 275 O VAL F 66 1555 1555 2.88
LINK K K E 275 O HOH F 292 1555 1555 2.99
SITE 1 AC1 4 GLU A 46 VAL A 66 GLU B 46 VAL B 66
SITE 1 AC2 7 GLY A 23 ARG A 27 ARG A 88 GLY A 90
SITE 2 AC2 7 SER A 91 IM5 A 501 ARG B 45
SITE 1 AC3 14 SER A 91 CYS A 92 GLY A 93 TYR A 160
SITE 2 AC3 14 VAL A 181 GLU A 182 MET A 183 GLU A 184
SITE 3 AC3 14 ASP A 206 TRP A 212 HOH A 281 HOH A 294
SITE 4 AC3 14 PO4 A 502 HIS B 7
SITE 1 AC4 7 ARG A 45 GLY B 23 ARG B 27 ARG B 88
SITE 2 AC4 7 GLY B 90 SER B 91 IM5 B 501
SITE 1 AC5 13 HIS A 7 SER B 91 CYS B 92 GLY B 93
SITE 2 AC5 13 TYR B 160 VAL B 181 GLU B 182 MET B 183
SITE 3 AC5 13 GLU B 184 ASP B 206 TRP B 212 HOH B 315
SITE 4 AC5 13 PO4 B 502
SITE 1 AC6 5 GLU C 46 VAL C 66 GLU D 46 VAL D 66
SITE 2 AC6 5 HOH D 291
SITE 1 AC7 7 GLY C 23 ARG C 27 ARG C 88 GLY C 90
SITE 2 AC7 7 SER C 91 IM5 C 501 ARG D 45
SITE 1 AC8 15 SER C 91 CYS C 92 GLY C 93 TYR C 160
SITE 2 AC8 15 VAL C 181 GLU C 182 MET C 183 GLU C 184
SITE 3 AC8 15 ASP C 206 TRP C 212 HOH C 297 HOH C 314
SITE 4 AC8 15 HOH C 320 PO4 C 502 HIS D 7
SITE 1 AC9 7 ARG C 45 GLY D 23 ARG D 27 ARG D 88
SITE 2 AC9 7 GLY D 90 SER D 91 IM5 D 501
SITE 1 BC1 16 HIS C 7 VAL D 66 SER D 91 CYS D 92
SITE 2 BC1 16 GLY D 93 TYR D 160 VAL D 181 GLU D 182
SITE 3 BC1 16 MET D 183 GLU D 184 ASP D 206 TRP D 212
SITE 4 BC1 16 HOH D 282 HOH D 284 HOH D 300 PO4 D 502
SITE 1 BC2 6 GLU E 46 VAL E 66 HOH E 293 GLU F 46
SITE 2 BC2 6 VAL F 66 HOH F 292
SITE 1 BC3 7 GLY E 23 ARG E 27 ARG E 88 GLY E 90
SITE 2 BC3 7 SER E 91 IM5 E 501 ARG F 45
SITE 1 BC4 17 VAL E 66 SER E 91 CYS E 92 GLY E 93
SITE 2 BC4 17 TYR E 160 VAL E 181 GLU E 182 MET E 183
SITE 3 BC4 17 GLU E 184 ASP E 206 TRP E 212 HOH E 288
SITE 4 BC4 17 HOH E 309 HOH E 339 PO4 E 502 HIS F 7
SITE 5 BC4 17 HOH F 304
SITE 1 BC5 7 ARG E 45 GLY F 23 ARG F 27 ARG F 88
SITE 2 BC5 7 GLY F 90 SER F 91 IM5 F 501
SITE 1 BC6 14 HIS E 7 SER F 91 CYS F 92 GLY F 93
SITE 2 BC6 14 TYR F 160 VAL F 181 GLU F 182 MET F 183
SITE 3 BC6 14 GLU F 184 ASP F 206 TRP F 212 HOH F 287
SITE 4 BC6 14 HOH F 307 PO4 F 502
CRYST1 61.197 77.371 92.197 67.71 73.62 86.03 P 1 6
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 0.016341 -0.001135 -0.004724 0.00000
SCALE2 0.000000 0.012956 -0.005254 0.00000
SCALE3 0.000000 0.000000 0.012200 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
