HEADER CHAPERONE 26-OCT-10 3PEJ
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF AN HSP90 FROM PLASMODIUM
TITLE 2 FALCIPARUM, PFL1070C IN THE PRESENCE OF MACBECIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPLASMIN HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 GENE: PFL1070C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15MLH
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, HEAT SHOCK
KEYWDS 2 PROTEIN, CHAPERONE, ATP BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,W.TEMPEL,A.HUTCHINSON,J.WEADGE,F.MACKENZIE,
AUTHOR 2 G.SENISTERRA,M.VEDADI,D.COSSAR,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 3 J.WEIGELT,R.HUI,J.C.PIZZARO,T.HILLS,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 4 (SGC)
REVDAT 4 06-SEP-23 3PEJ 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3PEJ 1 REMARK
REVDAT 2 01-DEC-10 3PEJ 1 AUTHOR JRNL
REVDAT 1 17-NOV-10 3PEJ 0
JRNL AUTH A.K.WERNIMONT,W.TEMPEL,A.HUTCHINSON,J.WEADGE,F.MACKENZIE,
JRNL AUTH 2 G.SENISTERRA,M.VEDADI,D.COSSAR,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 3 C.BOUNTRA,J.WEIGELT,R.HUI,J.C.PIZZARO,T.HILLS
JRNL TITL CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF AN HSP90 FROM
JRNL TITL 2 PLASMODIUM FALCIPARUM, PFL1070C IN THE PRESENCE OF MACBECIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 19044
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 974
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2691
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2727
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2552
REMARK 3 BIN R VALUE (WORKING SET) : 0.2711
REMARK 3 BIN FREE R VALUE : 0.3028
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.17
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 70
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 95
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 75.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.07990
REMARK 3 B22 (A**2) : -1.07990
REMARK 3 B33 (A**2) : 2.15990
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.460
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4166 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 5644 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 1448 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 113 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 590 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 4084 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 587 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4688 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.31
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.10
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19268
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.810
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.99100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3PEH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % PEG 5K MME 0.2 M AMMONIUM SULFATE
REMARK 280 0.1 M MES PH 6.5 1 MM MECBECIN 4 MM MGCL2 2 MM TCEP ETHYLENE
REMARK 280 GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.44000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.84900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.44000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.44000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.84900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.44000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.44000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 79.84900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.44000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.44000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.84900
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 50
REMARK 465 HIS A 51
REMARK 465 HIS A 52
REMARK 465 HIS A 53
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 HIS A 56
REMARK 465 SER A 57
REMARK 465 SER A 58
REMARK 465 GLY A 59
REMARK 465 ARG A 60
REMARK 465 GLU A 61
REMARK 465 ASN A 62
REMARK 465 LEU A 63
REMARK 465 TYR A 64
REMARK 465 PHE A 65
REMARK 465 GLN A 66
REMARK 465 GLY A 67
REMARK 465 PRO A 68
REMARK 465 THR A 69
REMARK 465 GLU A 70
REMARK 465 SER A 71
REMARK 465 MET A 72
REMARK 465 MET B 50
REMARK 465 HIS B 51
REMARK 465 HIS B 52
REMARK 465 HIS B 53
REMARK 465 HIS B 54
REMARK 465 HIS B 55
REMARK 465 HIS B 56
REMARK 465 SER B 57
REMARK 465 SER B 58
REMARK 465 GLY B 59
REMARK 465 ARG B 60
REMARK 465 GLU B 61
REMARK 465 ASN B 62
REMARK 465 LEU B 63
REMARK 465 TYR B 64
REMARK 465 PHE B 65
REMARK 465 GLN B 66
REMARK 465 GLY B 67
REMARK 465 PRO B 68
REMARK 465 THR B 69
REMARK 465 GLU B 70
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 GLU A 73 CG CD OE1 OE2
REMARK 470 ILE A 88 CD1
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 SER A 123 OG
REMARK 470 GLU A 140 CD OE1 OE2
REMARK 470 LYS A 141 CE NZ
REMARK 470 ILE A 159 CG1 CG2 CD1
REMARK 470 ASN A 161 CG OD1 ND2
REMARK 470 LYS A 167 CE NZ
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 LYS A 238 CD CE NZ
REMARK 470 GLU A 249 CG CD OE1 OE2
REMARK 470 GLN A 269 CG CD OE1 NE2
REMARK 470 PHE A 270 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 293 CE NZ
REMARK 470 LYS A 305 CG CD CE NZ
REMARK 470 ASP A 310 CG OD1 OD2
REMARK 470 LYS A 315 CD CE NZ
REMARK 470 SER B 71 OG
REMARK 470 MET B 72 CG SD CE
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 GLN B 78 CG CD OE1 NE2
REMARK 470 SER B 120 OG
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 SER B 123 OG
REMARK 470 ASN B 160 CG OD1 ND2
REMARK 470 ASN B 161 CG OD1 ND2
REMARK 470 LYS B 225 CG CD CE NZ
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 GLU B 249 CG CD OE1 OE2
REMARK 470 LYS B 266 NZ
REMARK 470 GLN B 269 CG CD OE1 NE2
REMARK 470 PHE B 270 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 293 CG CD CE NZ
REMARK 470 LYS B 305 CG CD CE NZ
REMARK 470 ASP B 310 CG OD1 OD2
REMARK 470 LYS B 315 CE NZ
REMARK 470 LYS B 322 CE NZ
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 LYS A 96 -35.99 -37.51
REMARK 500 GLU A 122 1.72 -68.54
REMARK 500 THR A 149 51.06 -99.88
REMARK 500 ALA A 224 14.45 57.55
REMARK 500 LYS A 238 -63.41 73.69
REMARK 500 LYS B 96 -36.19 -37.78
REMARK 500 GLU B 122 1.91 -68.77
REMARK 500 THR B 149 50.73 -99.55
REMARK 500 ALA B 224 15.06 57.54
REMARK 500 LYS B 238 -63.32 73.61
REMARK 500 ALA B 251 22.03 -69.27
REMARK 500 ASP B 311 106.74 -48.63
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 BC2 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BC2 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PEH RELATED DB: PDB
DBREF 3PEJ A 68 330 UNP Q8I0V4 Q8I0V4_PLAF7 68 330
DBREF 3PEJ B 68 330 UNP Q8I0V4 Q8I0V4_PLAF7 68 330
SEQADV 3PEJ MET A 50 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 51 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 52 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 53 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 54 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 55 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS A 56 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ SER A 57 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ SER A 58 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLY A 59 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ ARG A 60 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLU A 61 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ ASN A 62 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ LEU A 63 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ TYR A 64 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ PHE A 65 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLN A 66 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLY A 67 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ MET B 50 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 51 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 52 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 53 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 54 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 55 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ HIS B 56 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ SER B 57 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ SER B 58 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLY B 59 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ ARG B 60 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLU B 61 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ ASN B 62 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ LEU B 63 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ TYR B 64 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ PHE B 65 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLN B 66 UNP Q8I0V4 EXPRESSION TAG
SEQADV 3PEJ GLY B 67 UNP Q8I0V4 EXPRESSION TAG
SEQRES 1 A 281 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 281 LEU TYR PHE GLN GLY PRO THR GLU SER MET GLU SER HIS
SEQRES 3 A 281 GLN TYR GLN THR GLU VAL THR ARG LEU MET ASP ILE ILE
SEQRES 4 A 281 VAL ASN SER LEU TYR THR GLN LYS GLU VAL PHE LEU ARG
SEQRES 5 A 281 GLU LEU ILE SER ASN ALA ALA ASP ALA LEU GLU LYS ILE
SEQRES 6 A 281 ARG PHE LEU SER LEU SER ASP GLU SER VAL LEU GLY GLU
SEQRES 7 A 281 GLU LYS LYS LEU GLU ILE ARG ILE SER ALA ASN LYS GLU
SEQRES 8 A 281 LYS ASN ILE LEU SER ILE THR ASP THR GLY ILE GLY MET
SEQRES 9 A 281 THR LYS VAL ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 10 A 281 LYS SER GLY THR SER ASN PHE LEU GLU ALA ILE SER LYS
SEQRES 11 A 281 SER GLY GLY ASP MET SER LEU ILE GLY GLN PHE GLY VAL
SEQRES 12 A 281 GLY PHE TYR SER ALA PHE LEU VAL ALA ASP LYS VAL ILE
SEQRES 13 A 281 VAL TYR THR LYS ASN ASN ASP ASP GLU GLN TYR ILE TRP
SEQRES 14 A 281 GLU SER THR ALA ASP ALA LYS PHE THR ILE TYR LYS ASP
SEQRES 15 A 281 PRO ARG GLY ALA THR LEU LYS ARG GLY THR ARG ILE SER
SEQRES 16 A 281 LEU HIS LEU LYS GLU ASP ALA THR ASN LEU LEU ASN ASP
SEQRES 17 A 281 LYS LYS LEU MET ASP LEU ILE SER LYS TYR SER GLN PHE
SEQRES 18 A 281 ILE GLN PHE PRO ILE TYR LEU LEU HIS GLU ASN VAL TYR
SEQRES 19 A 281 THR GLU GLU VAL LEU ALA ASP ILE ALA LYS ASP MET VAL
SEQRES 20 A 281 ASN ASP PRO ASN TYR ASP SER VAL LYS VAL GLU GLU THR
SEQRES 21 A 281 ASP ASP PRO ASN LYS LYS THR ARG THR VAL GLU LYS LYS
SEQRES 22 A 281 VAL LYS LYS TRP THR LEU MET ASN
SEQRES 1 B 281 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 B 281 LEU TYR PHE GLN GLY PRO THR GLU SER MET GLU SER HIS
SEQRES 3 B 281 GLN TYR GLN THR GLU VAL THR ARG LEU MET ASP ILE ILE
SEQRES 4 B 281 VAL ASN SER LEU TYR THR GLN LYS GLU VAL PHE LEU ARG
SEQRES 5 B 281 GLU LEU ILE SER ASN ALA ALA ASP ALA LEU GLU LYS ILE
SEQRES 6 B 281 ARG PHE LEU SER LEU SER ASP GLU SER VAL LEU GLY GLU
SEQRES 7 B 281 GLU LYS LYS LEU GLU ILE ARG ILE SER ALA ASN LYS GLU
SEQRES 8 B 281 LYS ASN ILE LEU SER ILE THR ASP THR GLY ILE GLY MET
SEQRES 9 B 281 THR LYS VAL ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 10 B 281 LYS SER GLY THR SER ASN PHE LEU GLU ALA ILE SER LYS
SEQRES 11 B 281 SER GLY GLY ASP MET SER LEU ILE GLY GLN PHE GLY VAL
SEQRES 12 B 281 GLY PHE TYR SER ALA PHE LEU VAL ALA ASP LYS VAL ILE
SEQRES 13 B 281 VAL TYR THR LYS ASN ASN ASP ASP GLU GLN TYR ILE TRP
SEQRES 14 B 281 GLU SER THR ALA ASP ALA LYS PHE THR ILE TYR LYS ASP
SEQRES 15 B 281 PRO ARG GLY ALA THR LEU LYS ARG GLY THR ARG ILE SER
SEQRES 16 B 281 LEU HIS LEU LYS GLU ASP ALA THR ASN LEU LEU ASN ASP
SEQRES 17 B 281 LYS LYS LEU MET ASP LEU ILE SER LYS TYR SER GLN PHE
SEQRES 18 B 281 ILE GLN PHE PRO ILE TYR LEU LEU HIS GLU ASN VAL TYR
SEQRES 19 B 281 THR GLU GLU VAL LEU ALA ASP ILE ALA LYS ASP MET VAL
SEQRES 20 B 281 ASN ASP PRO ASN TYR ASP SER VAL LYS VAL GLU GLU THR
SEQRES 21 B 281 ASP ASP PRO ASN LYS LYS THR ARG THR VAL GLU LYS LYS
SEQRES 22 B 281 VAL LYS LYS TRP THR LEU MET ASN
HET BC2 A1001 40
HET SO4 A 1 5
HET BC2 B1001 40
HET SO4 B 2 5
HET SO4 B 3 5
HETNAM BC2 MACBECIN
HETNAM SO4 SULFATE ION
FORMUL 3 BC2 2(C30 H42 N2 O8)
FORMUL 4 SO4 3(O4 S 2-)
HELIX 1 1 SER A 74 TYR A 93 1 20
HELIX 2 2 GLN A 95 GLU A 97 5 3
HELIX 3 3 VAL A 98 ASP A 121 1 24
HELIX 4 4 GLU A 122 LEU A 125 5 4
HELIX 5 5 THR A 154 LYS A 167 1 14
HELIX 6 6 GLY A 169 SER A 180 1 12
HELIX 7 7 VAL A 192 LEU A 199 5 8
HELIX 8 8 GLU A 249 LEU A 255 5 7
HELIX 9 9 ASN A 256 SER A 268 1 13
HELIX 10 10 ALA A 289 VAL A 296 1 8
HELIX 11 11 SER B 74 TYR B 93 1 20
HELIX 12 12 GLN B 95 GLU B 97 5 3
HELIX 13 13 VAL B 98 ASP B 121 1 24
HELIX 14 14 GLU B 122 LEU B 125 5 4
HELIX 15 15 THR B 154 LYS B 167 1 14
HELIX 16 16 GLY B 169 SER B 180 1 12
HELIX 17 17 VAL B 192 LEU B 199 5 8
HELIX 18 18 ASP B 250 LEU B 255 5 6
HELIX 19 19 ASN B 256 SER B 268 1 13
HELIX 20 20 ALA B 289 VAL B 296 1 8
SHEET 1 A 9 PHE A 226 LYS A 230 0
SHEET 2 A 9 GLN A 215 THR A 221 -1 N ILE A 217 O TYR A 229
SHEET 3 A 9 ALA A 201 LYS A 209 -1 N VAL A 206 O TRP A 218
SHEET 4 A 9 GLY A 240 LEU A 247 -1 O ARG A 242 N TYR A 207
SHEET 5 A 9 ILE A 143 ASP A 148 -1 N LEU A 144 O LEU A 245
SHEET 6 A 9 ILE A 133 ASN A 138 -1 N ARG A 134 O THR A 147
SHEET 7 A 9 ILE A 275 LEU A 288 1 O TYR A 276 N ILE A 135
SHEET 8 A 9 THR A 316 LEU A 328 -1 O LYS A 325 N HIS A 279
SHEET 9 A 9 SER A 303 VAL A 306 -1 N SER A 303 O LYS A 322
SHEET 1 B 9 PHE B 226 LYS B 230 0
SHEET 2 B 9 GLN B 215 THR B 221 -1 N ILE B 217 O TYR B 229
SHEET 3 B 9 ALA B 201 LYS B 209 -1 N VAL B 206 O TRP B 218
SHEET 4 B 9 GLY B 240 LEU B 247 -1 O ARG B 242 N TYR B 207
SHEET 5 B 9 ILE B 143 ASP B 148 -1 N LEU B 144 O LEU B 245
SHEET 6 B 9 ILE B 133 ASN B 138 -1 N ARG B 134 O THR B 147
SHEET 7 B 9 ILE B 275 LEU B 288 1 O TYR B 276 N ILE B 135
SHEET 8 B 9 THR B 316 LEU B 328 -1 O LYS B 325 N HIS B 279
SHEET 9 B 9 SER B 303 VAL B 306 -1 N SER B 303 O LYS B 322
SITE 1 AC1 11 ASP A 109 ALA A 110 ASP A 148 ASP A 157
SITE 2 AC1 11 ASN A 161 ILE A 165 GLY A 191 VAL A 192
SITE 3 AC1 11 GLY A 193 PHE A 194 THR A 241
SITE 1 AC2 11 ASP B 109 ALA B 110 ASP B 148 ASP B 157
SITE 2 AC2 11 ASN B 161 ILE B 165 GLY B 191 VAL B 192
SITE 3 AC2 11 GLY B 193 PHE B 194 THR B 241
SITE 1 AC3 3 ARG A 134 THR A 147 ARG A 242
SITE 1 AC4 3 ARG B 134 THR B 147 ARG B 242
SITE 1 AC5 4 ALA B 137 LYS B 139 GLU B 140 LYS B 324
CRYST1 96.880 96.880 159.698 90.00 90.00 90.00 P 42 21 2 16
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 0.010322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
