HEADER SIGNALING PROTEIN,TRANSFERASE/CELL CYCLE17-APR-07 2PK9
TITLE STRUCTURE OF THE PHO85-PHO80 CDK-CYCLIN COMPLEX OF THE PHOSPHATE-
TITLE 2 RESPONSIVE SIGNAL TRANSDUCTION PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT PROTEIN KINASE PHO85;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: SERINE/THREONINE-PROTEIN KINASE PHO85; NEGATIVE REGULATOR OF
COMPND 5 THE PHO SYSTEM;
COMPND 6 EC: 2.7.11.22;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PHO85 CYCLIN PHO80;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: PHOSPHATE SYSTEM CYCLIN PHO80; AMINOGLYCOSIDE ANTIBIOTIC
COMPND 12 SENSITIVITY PROTEIN 3;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: PHO85, SSG3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE60;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: PHO80, AGS3, TUP7, VAC5;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PSBET
KEYWDS CYCLIN-DEPENDENT KINASE, CYCLIN, SIGNALING PROTEIN, TRANSFERASE- CELL
KEYWDS 2 CYCLE COMPLEX, TRANSFERASE-CELL CYCLE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HUANG,I.FERRIN-O'CONNELL,W.ZHANG,G.A.LEONARD,E.K.O'SHEA,F.A.QUIOCHO
REVDAT 4 21-FEB-24 2PK9 1 REMARK SEQADV
REVDAT 3 24-JUL-19 2PK9 1 REMARK
REVDAT 2 24-FEB-09 2PK9 1 VERSN
REVDAT 1 11-DEC-07 2PK9 0
JRNL AUTH K.HUANG,I.FERRIN-O'CONNELL,W.ZHANG,G.A.LEONARD,E.K.O'SHEA,
JRNL AUTH 2 F.A.QUIOCHO
JRNL TITL STRUCTURE OF THE PHO85-PHO80 CDK-CYCLIN COMPLEX OF THE
JRNL TITL 2 PHOSPHATE-RESPONSIVE SIGNAL TRANSDUCTION PATHWAY
JRNL REF MOL.CELL V. 28 614 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 18042456
JRNL DOI 10.1016/J.MOLCEL.2007.09.013
REMARK 2
REMARK 2 RESOLUTION. 2.91 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) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 49532
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) : 0.283
REMARK 3 R VALUE (WORKING SET) : 0.281
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2622
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) : 2.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2749
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.3940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.14000
REMARK 3 B22 (A**2) : 5.14000
REMARK 3 B33 (A**2) : -7.71000
REMARK 3 B12 (A**2) : 2.57000
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): 0.575
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.388
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 : 0.862
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.819
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8055 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10916 ; 1.469 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 970 ; 6.515 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;39.747 ;23.704
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1400 ;18.716 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;18.569 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1248 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5975 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3689 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5433 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 217 ; 0.138 ; 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): 49 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.098 ; 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): 4921 ; 1.090 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7969 ; 1.334 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3134 ; 0.723 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2947 ; 1.237 ; 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: NULL
REMARK 4
REMARK 4 2PK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042470.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-05; 11-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 200; 200
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; ESRF
REMARK 200 BEAMLINE : 19-ID; ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97948; 0.97926
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : APS 19ID; ESRF ID29
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE; ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47431
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.906
REMARK 200 RESOLUTION RANGE LOW (A) : 15.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : 0.29000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9UL 12% PEG 10000, 10% GLYCEROL, 0.2UL
REMARK 280 0.25 M STRONTIUM CHLORIDE (SRCL2), 10 MM TRIS (2-CARBOXYETHYL)
REMARK 280 PHOSPHINE (TCEP, 0.1 M 2-MORPHOLINOETHANESULFONIC ACID (MES), PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 70.60833
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 141.21667
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 141.21667
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 70.60833
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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, 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9720 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 GLN A 6
REMARK 465 ASP A 41
REMARK 465 THR A 74
REMARK 465 GLU A 75
REMARK 465 VAL A 98
REMARK 465 GLY A 99
REMARK 465 ASN A 100
REMARK 465 THR A 101
REMARK 465 PRO A 102
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 ALA A 304
REMARK 465 SER A 305
REMARK 465 MET A 306
REMARK 465 GLY A 307
REMARK 465 GLY A 308
REMARK 465 SER A 309
REMARK 465 ARG A 310
REMARK 465 SER A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 SER B 3
REMARK 465 THR B 4
REMARK 465 SER B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 ARG B 8
REMARK 465 SER B 9
REMARK 465 GLU B 10
REMARK 465 ASN B 11
REMARK 465 ILE B 12
REMARK 465 HIS B 13
REMARK 465 GLU B 14
REMARK 465 ASP B 15
REMARK 465 GLN B 16
REMARK 465 ALA B 54
REMARK 465 THR B 55
REMARK 465 LYS B 56
REMARK 465 LYS B 57
REMARK 465 SER B 58
REMARK 465 ASP B 59
REMARK 465 ASP B 60
REMARK 465 GLN B 61
REMARK 465 ALA B 195
REMARK 465 LEU B 196
REMARK 465 GLY B 197
REMARK 465 SER B 198
REMARK 465 LEU B 199
REMARK 465 ASP B 200
REMARK 465 LEU B 201
REMARK 465 ASP B 202
REMARK 465 SER B 203
REMARK 465 TYR B 204
REMARK 465 ILE B 249
REMARK 465 ASP B 250
REMARK 465 ILE B 251
REMARK 465 VAL B 252
REMARK 465 SER B 253
REMARK 465 GLU B 254
REMARK 465 SER B 255
REMARK 465 GLY B 256
REMARK 465 SER B 257
REMARK 465 GLN B 258
REMARK 465 THR B 259
REMARK 465 THR B 260
REMARK 465 GLN B 261
REMARK 465 LEU B 262
REMARK 465 LYS B 263
REMARK 465 GLY B 264
REMARK 465 SER B 265
REMARK 465 SER B 266
REMARK 465 SER B 267
REMARK 465 PRO B 268
REMARK 465 ASN B 269
REMARK 465 SER B 270
REMARK 465 HIS B 271
REMARK 465 SER B 272
REMARK 465 SER B 273
REMARK 465 GLN B 274
REMARK 465 LYS B 275
REMARK 465 ARG B 276
REMARK 465 TYR B 277
REMARK 465 SER B 278
REMARK 465 GLU B 279
REMARK 465 ALA B 280
REMARK 465 LYS B 281
REMARK 465 ASP B 282
REMARK 465 ALA B 283
REMARK 465 HIS B 284
REMARK 465 ILE B 285
REMARK 465 TYR B 286
REMARK 465 ASN B 287
REMARK 465 LYS B 288
REMARK 465 ARG B 289
REMARK 465 SER B 290
REMARK 465 LYS B 291
REMARK 465 PRO B 292
REMARK 465 ASP B 293
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 SER C 4
REMARK 465 SER C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 14
REMARK 465 ASN C 15
REMARK 465 GLY C 16
REMARK 465 THR C 17
REMARK 465 TYR C 18
REMARK 465 LEU C 25
REMARK 465 ASN C 26
REMARK 465 LYS C 27
REMARK 465 THR C 28
REMARK 465 THR C 29
REMARK 465 GLY C 30
REMARK 465 VAL C 31
REMARK 465 TYR C 32
REMARK 465 LEU C 40
REMARK 465 ASP C 41
REMARK 465 SER C 42
REMARK 465 GLU C 43
REMARK 465 GLU C 44
REMARK 465 THR C 74
REMARK 465 GLU C 75
REMARK 465 ARG C 96
REMARK 465 THR C 97
REMARK 465 VAL C 98
REMARK 465 GLY C 99
REMARK 465 ASN C 100
REMARK 465 THR C 101
REMARK 465 PRO C 102
REMARK 465 ARG C 103
REMARK 465 TYR C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 ALA C 304
REMARK 465 SER C 305
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 GLY C 308
REMARK 465 SER C 309
REMARK 465 ARG C 310
REMARK 465 SER C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 HIS C 314
REMARK 465 HIS C 315
REMARK 465 HIS C 316
REMARK 465 HIS C 317
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 SER D 3
REMARK 465 THR D 4
REMARK 465 SER D 5
REMARK 465 GLY D 6
REMARK 465 GLU D 7
REMARK 465 ARG D 8
REMARK 465 SER D 9
REMARK 465 GLU D 10
REMARK 465 ASN D 11
REMARK 465 ILE D 12
REMARK 465 HIS D 13
REMARK 465 GLU D 14
REMARK 465 ASP D 15
REMARK 465 ALA D 54
REMARK 465 THR D 55
REMARK 465 LYS D 56
REMARK 465 LYS D 57
REMARK 465 SER D 58
REMARK 465 ASP D 59
REMARK 465 ASP D 60
REMARK 465 ALA D 195
REMARK 465 LEU D 196
REMARK 465 GLY D 197
REMARK 465 SER D 198
REMARK 465 LEU D 199
REMARK 465 ASP D 200
REMARK 465 LEU D 201
REMARK 465 ASP D 202
REMARK 465 SER D 203
REMARK 465 ILE D 251
REMARK 465 VAL D 252
REMARK 465 SER D 253
REMARK 465 GLU D 254
REMARK 465 SER D 255
REMARK 465 GLY D 256
REMARK 465 SER D 257
REMARK 465 GLN D 258
REMARK 465 THR D 259
REMARK 465 THR D 260
REMARK 465 GLN D 261
REMARK 465 LEU D 262
REMARK 465 LYS D 263
REMARK 465 GLY D 264
REMARK 465 SER D 265
REMARK 465 SER D 266
REMARK 465 SER D 267
REMARK 465 PRO D 268
REMARK 465 ASN D 269
REMARK 465 SER D 270
REMARK 465 HIS D 271
REMARK 465 SER D 272
REMARK 465 SER D 273
REMARK 465 GLN D 274
REMARK 465 LYS D 275
REMARK 465 ARG D 276
REMARK 465 TYR D 277
REMARK 465 SER D 278
REMARK 465 GLU D 279
REMARK 465 ALA D 280
REMARK 465 LYS D 281
REMARK 465 ASP D 282
REMARK 465 ALA D 283
REMARK 465 HIS D 284
REMARK 465 ILE D 285
REMARK 465 TYR D 286
REMARK 465 ASN D 287
REMARK 465 LYS D 288
REMARK 465 ARG D 289
REMARK 465 SER D 290
REMARK 465 LYS D 291
REMARK 465 PRO D 292
REMARK 465 ASP D 293
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 8 CG CD CE NZ
REMARK 480 GLN A 9 CB CG CD OE1 NE2
REMARK 480 LYS A 12 CG CD CE NZ
REMARK 480 THR A 17 OG1 CG2
REMARK 480 TYR A 18 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 THR A 20 OG1 CG2
REMARK 480 GLU A 37 CG CD OE1 OE2
REMARK 480 GLU A 43 CB CG CD OE1 OE2
REMARK 480 LYS A 77 CG CD CE NZ
REMARK 480 ASP A 86 CG OD1 OD2
REMARK 480 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 143 CG CD CE NZ
REMARK 480 GLN A 247 CG CD OE1 NE2
REMARK 480 HIS A 261 CG ND1 CD2 CE1 NE2
REMARK 480 LYS A 263 CG CD CE NZ
REMARK 480 ILE B 62 CG1 CG2 CD1
REMARK 480 LYS B 185 CG CD CE NZ
REMARK 480 LYS C 8 CG CD CE NZ
REMARK 480 LEU C 10 CG CD1 CD2
REMARK 480 GLU C 11 CG CD OE1 OE2
REMARK 480 LYS C 12 CG CD CE NZ
REMARK 480 LEU C 13 CG CD1 CD2
REMARK 480 TYR C 22 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 ASN C 76 CG OD1 ND2
REMARK 480 LYS C 77 CG CD CE NZ
REMARK 480 LYS C 143 CG CD CE NZ
REMARK 480 GLN C 247 CG CD OE1 NE2
REMARK 480 LYS C 263 CG CD CE NZ
REMARK 480 GLN D 16 CG CD OE1 NE2
REMARK 480 LYS D 185 CG CD CE NZ
REMARK 480 ASN D 208 CG OD1 ND2
REMARK 480 ASN D 248 CG OD1 ND2
REMARK 480 ILE D 249 CB CG1 CG2 CD1
REMARK 480 ASP D 250 CG OD1 OD2
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 CE1 TYR A 18 CG1 VAL A 38 1.98
REMARK 500 NZ LYS A 206 CD2 HIS A 261 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 112 CG1 ILE D 249 4655 1.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 261 CB HIS A 261 CG -0.139
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 261 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 TYR C 22 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR C 22 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP D 250 CB - CG - OD1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP D 250 CB - CG - OD2 ANGL. DEV. = 10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 10 45.82 -146.99
REMARK 500 GLU A 11 124.49 136.59
REMARK 500 THR A 28 -63.03 -130.60
REMARK 500 PRO A 47 108.57 -27.70
REMARK 500 ASN A 87 -156.02 -136.83
REMARK 500 ARG A 132 -15.14 76.04
REMARK 500 ASP A 133 47.36 -144.89
REMARK 500 LEU A 139 78.03 -116.38
REMARK 500 ASP A 151 80.32 53.07
REMARK 500 PHE A 152 41.86 -96.45
REMARK 500 PRO A 161 71.98 -67.54
REMARK 500 SER A 187 -147.84 -107.94
REMARK 500 LEU A 232 56.15 -101.69
REMARK 500 TRP A 233 67.26 170.06
REMARK 500 LYS A 241 30.55 -95.00
REMARK 500 LEU A 278 50.56 -106.13
REMARK 500 GLU B 51 -61.42 -91.54
REMARK 500 ASN B 52 61.73 -66.69
REMARK 500 SER B 116 -1.38 -53.49
REMARK 500 ALA B 119 -73.23 -44.55
REMARK 500 THR B 127 -55.01 -19.73
REMARK 500 ASN B 208 -17.15 65.93
REMARK 500 LYS B 211 29.98 48.35
REMARK 500 LEU B 227 -77.64 -81.94
REMARK 500 ALA B 233 -56.46 -139.28
REMARK 500 SER B 234 -43.45 159.19
REMARK 500 PRO B 246 134.72 -39.19
REMARK 500 LEU C 10 -145.29 -115.61
REMARK 500 TYR C 22 -148.93 -102.77
REMARK 500 GLU C 63 -7.79 -58.21
REMARK 500 ASN C 87 -153.72 -157.03
REMARK 500 ASP C 133 58.80 -152.40
REMARK 500 ASP C 151 80.74 55.31
REMARK 500 SER C 187 -156.29 -134.86
REMARK 500 THR C 188 -52.88 -17.26
REMARK 500 TRP C 233 78.52 -154.88
REMARK 500 LYS C 241 32.55 -98.12
REMARK 500 PRO C 251 107.29 -47.86
REMARK 500 ASP C 253 100.53 -56.73
REMARK 500 LYS C 263 41.53 -83.85
REMARK 500 HIS C 293 79.07 -111.99
REMARK 500 PRO D 19 129.00 -39.39
REMARK 500 LEU D 117 -26.16 -156.12
REMARK 500 TYR D 168 16.09 52.85
REMARK 500 PRO D 172 82.01 -68.98
REMARK 500 LYS D 193 -164.31 -71.33
REMARK 500 SER D 205 118.28 178.45
REMARK 500 ASN D 208 -40.88 76.06
REMARK 500 PHE D 231 18.70 -63.78
REMARK 500 ASN D 232 63.47 -113.84
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
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 MES B 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 294
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PMI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH ATP-GAMMA-S
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE WARNING: RESIDUE (D GLN 16 ) AND RESIDUE (D GLY 17 )
REMARK 999 ARE NOT LINKED.
REMARK 999 DISTANCE OF C-N BOND IS 2.46
DBREF 2PK9 A 1 305 UNP P17157 PHO85_YEAST 1 305
DBREF 2PK9 C 1 305 UNP P17157 PHO85_YEAST 1 305
DBREF 2PK9 B 1 293 UNP P20052 PHO80_YEAST 1 293
DBREF 2PK9 D 1 293 UNP P20052 PHO80_YEAST 1 293
SEQADV 2PK9 MET A 306 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 GLY A 307 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 GLY A 308 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 SER A 309 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 ARG A 310 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 SER A 311 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 312 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 313 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 314 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 315 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 316 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS A 317 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 MET C 306 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 GLY C 307 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 GLY C 308 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 SER C 309 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 ARG C 310 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 SER C 311 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 312 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 313 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 314 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 315 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 316 UNP P17157 EXPRESSION TAG
SEQADV 2PK9 HIS C 317 UNP P17157 EXPRESSION TAG
SEQRES 1 A 317 MET SER SER SER SER GLN PHE LYS GLN LEU GLU LYS LEU
SEQRES 2 A 317 GLY ASN GLY THR TYR ALA THR VAL TYR LYS GLY LEU ASN
SEQRES 3 A 317 LYS THR THR GLY VAL TYR VAL ALA LEU LYS GLU VAL LYS
SEQRES 4 A 317 LEU ASP SER GLU GLU GLY THR PRO SER THR ALA ILE ARG
SEQRES 5 A 317 GLU ILE SER LEU MET LYS GLU LEU LYS HIS GLU ASN ILE
SEQRES 6 A 317 VAL ARG LEU TYR ASP VAL ILE HIS THR GLU ASN LYS LEU
SEQRES 7 A 317 THR LEU VAL PHE GLU PHE MET ASP ASN ASP LEU LYS LYS
SEQRES 8 A 317 TYR MET ASP SER ARG THR VAL GLY ASN THR PRO ARG GLY
SEQRES 9 A 317 LEU GLU LEU ASN LEU VAL LYS TYR PHE GLN TRP GLN LEU
SEQRES 10 A 317 LEU GLN GLY LEU ALA PHE CYS HIS GLU ASN LYS ILE LEU
SEQRES 11 A 317 HIS ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN LYS
SEQRES 12 A 317 ARG GLY GLN LEU LYS LEU GLY ASP PHE GLY LEU ALA ARG
SEQRES 13 A 317 ALA PHE GLY ILE PRO VAL ASN THR PHE SER SER GLU VAL
SEQRES 14 A 317 VAL THR LEU TRP TYR ARG ALA PRO ASP VAL LEU MET GLY
SEQRES 15 A 317 SER ARG THR TYR SER THR SER ILE ASP ILE TRP SER CYS
SEQRES 16 A 317 GLY CYS ILE LEU ALA GLU MET ILE THR GLY LYS PRO LEU
SEQRES 17 A 317 PHE PRO GLY THR ASN ASP GLU GLU GLN LEU LYS LEU ILE
SEQRES 18 A 317 PHE ASP ILE MET GLY THR PRO ASN GLU SER LEU TRP PRO
SEQRES 19 A 317 SER VAL THR LYS LEU PRO LYS TYR ASN PRO ASN ILE GLN
SEQRES 20 A 317 GLN ARG PRO PRO ARG ASP LEU ARG GLN VAL LEU GLN PRO
SEQRES 21 A 317 HIS THR LYS GLU PRO LEU ASP GLY ASN LEU MET ASP PHE
SEQRES 22 A 317 LEU HIS GLY LEU LEU GLN LEU ASN PRO ASP MET ARG LEU
SEQRES 23 A 317 SER ALA LYS GLN ALA LEU HIS HIS PRO TRP PHE ALA GLU
SEQRES 24 A 317 TYR TYR HIS HIS ALA SER MET GLY GLY SER ARG SER HIS
SEQRES 25 A 317 HIS HIS HIS HIS HIS
SEQRES 1 B 293 MET GLU SER THR SER GLY GLU ARG SER GLU ASN ILE HIS
SEQRES 2 B 293 GLU ASP GLN GLY ILE PRO LYS VAL ILE LEU PRO ALA ASP
SEQRES 3 B 293 PHE ASN LYS CYS SER ARG THR ASP LEU VAL VAL LEU ILE
SEQRES 4 B 293 SER ARG MET LEU VAL SER LEU ILE ALA ILE ASN GLU ASN
SEQRES 5 B 293 SER ALA THR LYS LYS SER ASP ASP GLN ILE THR LEU THR
SEQRES 6 B 293 ARG TYR HIS SER LYS ILE PRO PRO ASN ILE SER ILE PHE
SEQRES 7 B 293 ASN TYR PHE ILE ARG LEU THR LYS PHE SER SER LEU GLU
SEQRES 8 B 293 HIS CYS VAL LEU MET THR SER LEU TYR TYR ILE ASP LEU
SEQRES 9 B 293 LEU GLN THR VAL TYR PRO ASP PHE THR LEU ASN SER LEU
SEQRES 10 B 293 THR ALA HIS ARG PHE LEU LEU THR ALA THR THR VAL ALA
SEQRES 11 B 293 THR LYS GLY LEU CYS ASP SER PHE SER THR ASN ALA HIS
SEQRES 12 B 293 TYR ALA LYS VAL GLY GLY VAL ARG CYS HIS GLU LEU ASN
SEQRES 13 B 293 ILE LEU GLU ASN ASP PHE LEU LYS ARG VAL ASN TYR ARG
SEQRES 14 B 293 ILE ILE PRO ARG ASP HIS ASN ILE THR LEU CYS SER ILE
SEQRES 15 B 293 GLU GLN LYS GLN LYS LYS PHE VAL ILE ASP LYS ASN ALA
SEQRES 16 B 293 LEU GLY SER LEU ASP LEU ASP SER TYR SER TYR VAL ASN
SEQRES 17 B 293 ARG PRO LYS SER GLY TYR ASN VAL LEU ASP LYS TYR TYR
SEQRES 18 B 293 ARG ARG ILE VAL GLN LEU VAL GLY SER PHE ASN ALA SER
SEQRES 19 B 293 PRO ASP LYS SER ARG LYS VAL ASP TYR VAL LEU PRO PRO
SEQRES 20 B 293 ASN ILE ASP ILE VAL SER GLU SER GLY SER GLN THR THR
SEQRES 21 B 293 GLN LEU LYS GLY SER SER SER PRO ASN SER HIS SER SER
SEQRES 22 B 293 GLN LYS ARG TYR SER GLU ALA LYS ASP ALA HIS ILE TYR
SEQRES 23 B 293 ASN LYS ARG SER LYS PRO ASP
SEQRES 1 C 317 MET SER SER SER SER GLN PHE LYS GLN LEU GLU LYS LEU
SEQRES 2 C 317 GLY ASN GLY THR TYR ALA THR VAL TYR LYS GLY LEU ASN
SEQRES 3 C 317 LYS THR THR GLY VAL TYR VAL ALA LEU LYS GLU VAL LYS
SEQRES 4 C 317 LEU ASP SER GLU GLU GLY THR PRO SER THR ALA ILE ARG
SEQRES 5 C 317 GLU ILE SER LEU MET LYS GLU LEU LYS HIS GLU ASN ILE
SEQRES 6 C 317 VAL ARG LEU TYR ASP VAL ILE HIS THR GLU ASN LYS LEU
SEQRES 7 C 317 THR LEU VAL PHE GLU PHE MET ASP ASN ASP LEU LYS LYS
SEQRES 8 C 317 TYR MET ASP SER ARG THR VAL GLY ASN THR PRO ARG GLY
SEQRES 9 C 317 LEU GLU LEU ASN LEU VAL LYS TYR PHE GLN TRP GLN LEU
SEQRES 10 C 317 LEU GLN GLY LEU ALA PHE CYS HIS GLU ASN LYS ILE LEU
SEQRES 11 C 317 HIS ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN LYS
SEQRES 12 C 317 ARG GLY GLN LEU LYS LEU GLY ASP PHE GLY LEU ALA ARG
SEQRES 13 C 317 ALA PHE GLY ILE PRO VAL ASN THR PHE SER SER GLU VAL
SEQRES 14 C 317 VAL THR LEU TRP TYR ARG ALA PRO ASP VAL LEU MET GLY
SEQRES 15 C 317 SER ARG THR TYR SER THR SER ILE ASP ILE TRP SER CYS
SEQRES 16 C 317 GLY CYS ILE LEU ALA GLU MET ILE THR GLY LYS PRO LEU
SEQRES 17 C 317 PHE PRO GLY THR ASN ASP GLU GLU GLN LEU LYS LEU ILE
SEQRES 18 C 317 PHE ASP ILE MET GLY THR PRO ASN GLU SER LEU TRP PRO
SEQRES 19 C 317 SER VAL THR LYS LEU PRO LYS TYR ASN PRO ASN ILE GLN
SEQRES 20 C 317 GLN ARG PRO PRO ARG ASP LEU ARG GLN VAL LEU GLN PRO
SEQRES 21 C 317 HIS THR LYS GLU PRO LEU ASP GLY ASN LEU MET ASP PHE
SEQRES 22 C 317 LEU HIS GLY LEU LEU GLN LEU ASN PRO ASP MET ARG LEU
SEQRES 23 C 317 SER ALA LYS GLN ALA LEU HIS HIS PRO TRP PHE ALA GLU
SEQRES 24 C 317 TYR TYR HIS HIS ALA SER MET GLY GLY SER ARG SER HIS
SEQRES 25 C 317 HIS HIS HIS HIS HIS
SEQRES 1 D 293 MET GLU SER THR SER GLY GLU ARG SER GLU ASN ILE HIS
SEQRES 2 D 293 GLU ASP GLN GLY ILE PRO LYS VAL ILE LEU PRO ALA ASP
SEQRES 3 D 293 PHE ASN LYS CYS SER ARG THR ASP LEU VAL VAL LEU ILE
SEQRES 4 D 293 SER ARG MET LEU VAL SER LEU ILE ALA ILE ASN GLU ASN
SEQRES 5 D 293 SER ALA THR LYS LYS SER ASP ASP GLN ILE THR LEU THR
SEQRES 6 D 293 ARG TYR HIS SER LYS ILE PRO PRO ASN ILE SER ILE PHE
SEQRES 7 D 293 ASN TYR PHE ILE ARG LEU THR LYS PHE SER SER LEU GLU
SEQRES 8 D 293 HIS CYS VAL LEU MET THR SER LEU TYR TYR ILE ASP LEU
SEQRES 9 D 293 LEU GLN THR VAL TYR PRO ASP PHE THR LEU ASN SER LEU
SEQRES 10 D 293 THR ALA HIS ARG PHE LEU LEU THR ALA THR THR VAL ALA
SEQRES 11 D 293 THR LYS GLY LEU CYS ASP SER PHE SER THR ASN ALA HIS
SEQRES 12 D 293 TYR ALA LYS VAL GLY GLY VAL ARG CYS HIS GLU LEU ASN
SEQRES 13 D 293 ILE LEU GLU ASN ASP PHE LEU LYS ARG VAL ASN TYR ARG
SEQRES 14 D 293 ILE ILE PRO ARG ASP HIS ASN ILE THR LEU CYS SER ILE
SEQRES 15 D 293 GLU GLN LYS GLN LYS LYS PHE VAL ILE ASP LYS ASN ALA
SEQRES 16 D 293 LEU GLY SER LEU ASP LEU ASP SER TYR SER TYR VAL ASN
SEQRES 17 D 293 ARG PRO LYS SER GLY TYR ASN VAL LEU ASP LYS TYR TYR
SEQRES 18 D 293 ARG ARG ILE VAL GLN LEU VAL GLY SER PHE ASN ALA SER
SEQRES 19 D 293 PRO ASP LYS SER ARG LYS VAL ASP TYR VAL LEU PRO PRO
SEQRES 20 D 293 ASN ILE ASP ILE VAL SER GLU SER GLY SER GLN THR THR
SEQRES 21 D 293 GLN LEU LYS GLY SER SER SER PRO ASN SER HIS SER SER
SEQRES 22 D 293 GLN LYS ARG TYR SER GLU ALA LYS ASP ALA HIS ILE TYR
SEQRES 23 D 293 ASN LYS ARG SER LYS PRO ASP
HET MES B 294 12
HET MES D 294 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 5 MES 2(C6 H13 N O4 S)
HELIX 1 1 PRO A 47 LYS A 58 1 12
HELIX 2 2 LEU A 89 SER A 95 1 7
HELIX 3 3 GLU A 106 ASN A 127 1 22
HELIX 4 4 LYS A 135 GLN A 137 5 3
HELIX 5 5 ASP A 178 GLY A 182 5 5
HELIX 6 6 SER A 189 GLY A 205 1 17
HELIX 7 7 ASN A 213 GLY A 226 1 14
HELIX 8 8 TRP A 233 LEU A 239 5 7
HELIX 9 9 LEU A 254 GLN A 259 1 6
HELIX 10 10 PRO A 260 THR A 262 5 3
HELIX 11 11 ASP A 267 LEU A 278 1 12
HELIX 12 12 ASN A 281 ARG A 285 5 5
HELIX 13 13 SER A 287 LEU A 292 1 6
HELIX 14 14 HIS A 293 TYR A 301 5 9
HELIX 15 15 ASP B 26 CYS B 30 5 5
HELIX 16 16 SER B 31 ASN B 52 1 22
HELIX 17 17 SER B 76 SER B 89 1 14
HELIX 18 18 GLU B 91 TYR B 109 1 19
HELIX 19 19 THR B 118 CYS B 135 1 18
HELIX 20 20 THR B 140 GLY B 149 1 10
HELIX 21 21 ARG B 151 VAL B 166 1 16
HELIX 22 22 HIS B 175 GLU B 183 1 9
HELIX 23 23 ARG B 209 TYR B 214 5 6
HELIX 24 24 ASN B 215 LEU B 227 1 13
HELIX 25 25 PRO C 47 LEU C 60 1 14
HELIX 26 26 LEU C 89 ASP C 94 1 6
HELIX 27 27 GLU C 106 ASN C 127 1 22
HELIX 28 28 LYS C 135 GLN C 137 5 3
HELIX 29 29 ALA C 176 MET C 181 1 6
HELIX 30 30 THR C 188 GLY C 205 1 18
HELIX 31 31 ASN C 213 GLY C 226 1 14
HELIX 32 32 TRP C 233 LEU C 239 5 7
HELIX 33 33 ASP C 253 GLN C 259 1 7
HELIX 34 34 PRO C 260 THR C 262 5 3
HELIX 35 35 ASP C 267 LEU C 278 1 12
HELIX 36 36 ASN C 281 ARG C 285 5 5
HELIX 37 37 SER C 287 LEU C 292 1 6
HELIX 38 38 ASP D 26 CYS D 30 5 5
HELIX 39 39 SER D 31 ASN D 52 1 22
HELIX 40 40 SER D 76 SER D 88 1 13
HELIX 41 41 GLU D 91 VAL D 108 1 18
HELIX 42 42 THR D 118 CYS D 135 1 18
HELIX 43 43 THR D 140 GLY D 149 1 10
HELIX 44 44 ARG D 151 VAL D 166 1 16
HELIX 45 45 HIS D 175 GLU D 183 1 9
HELIX 46 46 ARG D 209 TYR D 214 5 6
HELIX 47 47 ASN D 215 GLY D 229 1 15
SHEET 1 A 5 LYS A 12 GLY A 14 0
SHEET 2 A 5 ALA A 19 LEU A 25 -1 O VAL A 21 N LEU A 13
SHEET 3 A 5 TYR A 32 LYS A 39 -1 O VAL A 33 N GLY A 24
SHEET 4 A 5 LYS A 77 GLU A 83 -1 O PHE A 82 N ALA A 34
SHEET 5 A 5 LEU A 68 ILE A 72 -1 N TYR A 69 O VAL A 81
SHEET 1 B 3 ASN A 87 ASP A 88 0
SHEET 2 B 3 LEU A 139 ILE A 141 -1 O ILE A 141 N ASN A 87
SHEET 3 B 3 LEU A 147 LEU A 149 -1 O LYS A 148 N LEU A 140
SHEET 1 C 2 ILE A 129 LEU A 130 0
SHEET 2 C 2 ARG A 156 ALA A 157 -1 O ARG A 156 N LEU A 130
SHEET 1 D 2 LYS B 20 ILE B 22 0
SHEET 2 D 2 ASP B 242 VAL B 244 1 O VAL B 244 N VAL B 21
SHEET 1 E 4 THR C 20 VAL C 21 0
SHEET 2 E 4 ALA C 34 VAL C 38 -1 O GLU C 37 N THR C 20
SHEET 3 E 4 LEU C 78 PHE C 82 -1 O LEU C 80 N LYS C 36
SHEET 4 E 4 LEU C 68 VAL C 71 -1 N TYR C 69 O VAL C 81
SHEET 1 F 3 ASN C 87 ASP C 88 0
SHEET 2 F 3 LEU C 139 ILE C 141 -1 O ILE C 141 N ASN C 87
SHEET 3 F 3 LEU C 147 LEU C 149 -1 O LYS C 148 N LEU C 140
SHEET 1 G 2 ILE C 129 LEU C 130 0
SHEET 2 G 2 ARG C 156 ALA C 157 -1 O ARG C 156 N LEU C 130
SHEET 1 H 2 LYS D 20 ILE D 22 0
SHEET 2 H 2 ASP D 242 VAL D 244 1 O ASP D 242 N VAL D 21
SITE 1 AC1 8 ILE B 75 TYR B 80 ARG B 83 GLY B 148
SITE 2 AC1 8 GLY B 149 VAL B 150 PRO C 240 LYS C 241
SITE 1 AC2 10 GLY A 182 PRO A 240 LYS A 241 ILE D 75
SITE 2 AC2 10 TYR D 80 ARG D 83 HIS D 120 ARG D 121
SITE 3 AC2 10 GLY D 148 GLY D 149
CRYST1 147.775 147.775 211.825 90.00 90.00 120.00 P 31 2 1 12
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 0.006767 0.003907 0.000000 0.00000
SCALE2 0.000000 0.007814 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
