HEADER PROTEIN TRANSPORT 30-SEP-10 3P1W
TITLE CRYSTAL STRUCTURE OF RAB GDI FROM PLASMODIUM FALCIPARUM, PFL2060C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RABGDI PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 GENE: PFL2060C;
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: PET15
KEYWDS GDI RAB, MALARIA, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSPORT,
KEYWDS 2 PF10_0345, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,A.M.NECULAI,J.WEADGE,F.MACKENZIE,D.COSSAR,W.TEMPEL,
AUTHOR 2 A.BOCHKAREV,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,G.LANGSLEY,J.BOSCH,
AUTHOR 3 R.HUI,J.C.PIZZARO,A.HUTCHINSON,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-SEP-23 3P1W 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3P1W 1 REMARK
REVDAT 2 29-OCT-14 3P1W 1 AUTHOR JRNL VERSN
REVDAT 1 15-DEC-10 3P1W 0
JRNL AUTH A.K.WERNIMONT,A.M.NECULAI,J.WEADGE,F.MACKENZIE,D.COSSAR,
JRNL AUTH 2 W.TEMPEL,A.BOCHKAREV,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
JRNL AUTH 3 G.LANGSLEY,J.BOSCH,R.HUI,J.C.PIZZARO,A.HUTCHINSON
JRNL TITL CRYSTAL STRUCTURE OF RAB GDI FROM PLASMODIUM FALCIPARUM,
JRNL TITL 2 PFL2060C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.ATTAL,G.LANGSLEY
REMARK 1 TITL A PLASMODIUM FALCIPARUM HOMOLOGUE OF A RAB SPECIFIC GDP
REMARK 1 TITL 2 DISSOCIATION INHIBITOR.
REMARK 1 REF MOL.BIOCHEM.PARASITOL. V. 79 91 1996
REMARK 1 REFN ISSN 0166-6851
REMARK 1 PMID 8844675
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 50360
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2571
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3439
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3523
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -2.03000
REMARK 3 B33 (A**2) : 1.41000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.216
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3698 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2444 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5039 ; 1.264 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6024 ; 0.872 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 461 ; 5.667 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;35.649 ;25.427
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 644 ;12.435 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;12.808 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 568 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4105 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 715 ; 0.001 ; 0.020
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): 2256 ; 0.667 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 909 ; 0.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3679 ; 1.195 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1442 ; 1.799 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1357 ; 2.904 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4039 14.5863 44.0026
REMARK 3 T TENSOR
REMARK 3 T11: 0.0697 T22: 0.0721
REMARK 3 T33: 0.0317 T12: 0.0521
REMARK 3 T13: -0.0073 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.5942 L22: 1.4950
REMARK 3 L33: 1.0229 L12: -0.5137
REMARK 3 L13: -0.1015 L23: 0.4588
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: 0.3067 S13: -0.0218
REMARK 3 S21: -0.1596 S22: -0.1369 S23: 0.0740
REMARK 3 S31: -0.0253 S32: -0.0490 S33: 0.0040
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3P1W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57819
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.98900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.570
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 1LV0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1 M HEPES 7.5, 0.2 M
REMARK 280 NACL2, 2 MM TCEP, 5% MPD, GLYCEROL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 62.95800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.95800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.44250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.28250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.44250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.28250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.95800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.44250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.28250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.95800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.44250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.28250
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 ARG A -5
REMARK 465 GLU A -4
REMARK 465 ASN A -3
REMARK 465 LEU A -2
REMARK 465 TYR A -1
REMARK 465 PHE A 0
REMARK 465 GLY A 254
REMARK 465 GLY A 255
REMARK 465 ASP A 445
REMARK 465 ASP A 446
REMARK 465 LEU A 447
REMARK 465 ASN A 448
REMARK 465 THR A 449
REMARK 465 ASN A 450
REMARK 465 ALA A 451
REMARK 465 ASP A 452
REMARK 465 GLY A 453
REMARK 465 GLU A 454
REMARK 465 ALA A 455
REMARK 465 PRO A 456
REMARK 465 ASP A 457
REMARK 465 PHE A 458
REMARK 465 ASN A 459
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 GLN A 1 CG CD OE1 NE2
REMARK 470 ARG A 94 CD NE CZ NH1 NH2
REMARK 470 MET A 143 CG SD CE
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 181 CE NZ
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 253 CG OD1 ND2
REMARK 470 LYS A 359 CE NZ
REMARK 470 LYS A 377 CE NZ
REMARK 470 LYS A 381 CD CE NZ
REMARK 470 LYS A 405 CG CD CE NZ
REMARK 470 LYS A 406 CD CE NZ
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 MET A 143 CB
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 MET A 143 CA MET A 143 CB 0.210
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 MET A 143 -60.82 103.40
REMARK 500 SER A 351 -159.41 -157.83
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3P1W A 3 459 UNP Q8I501 Q8I501_PLAF7 3 459
SEQADV 3P1W MET A -15 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -14 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -13 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -12 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -11 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -10 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W HIS A -9 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W SER A -8 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W SER A -7 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W GLY A -6 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W ARG A -5 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W GLU A -4 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W ASN A -3 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W LEU A -2 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W TYR A -1 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W PHE A 0 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W GLN A 1 UNP Q8I501 EXPRESSION TAG
SEQADV 3P1W GLY A 2 UNP Q8I501 EXPRESSION TAG
SEQRES 1 A 475 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 475 LEU TYR PHE GLN GLY GLU HIS TYR ASP VAL ILE ILE LEU
SEQRES 3 A 475 GLY THR GLY LEU LYS GLU CYS ILE LEU SER GLY LEU LEU
SEQRES 4 A 475 SER HIS TYR GLY LYS LYS ILE LEU VAL LEU ASP ARG ASN
SEQRES 5 A 475 PRO TYR TYR GLY GLY GLU THR ALA SER LEU ASN LEU THR
SEQRES 6 A 475 ASN LEU TYR ASN THR PHE LYS PRO LYS GLU ASN ILE PRO
SEQRES 7 A 475 SER LYS TYR GLY GLU ASN ARG HIS TRP ASN VAL ASP LEU
SEQRES 8 A 475 ILE PRO LYS PHE ILE LEU VAL GLY GLY ASN LEU VAL LYS
SEQRES 9 A 475 ILE LEU LYS LYS THR ARG VAL THR ASN TYR LEU GLU TRP
SEQRES 10 A 475 LEU VAL VAL GLU GLY SER TYR VAL TYR GLN HIS GLN LYS
SEQRES 11 A 475 LYS GLY PHE LEU THR SER GLU LYS PHE ILE HIS LYS VAL
SEQRES 12 A 475 PRO ALA THR ASP MET GLU ALA LEU VAL SER PRO LEU LEU
SEQRES 13 A 475 SER LEU MET GLU LYS ASN ARG CYS LYS ASN PHE TYR GLN
SEQRES 14 A 475 TYR VAL SER GLU TRP ASP ALA ASN LYS ARG ASN THR TRP
SEQRES 15 A 475 ASP ASN LEU ASP PRO TYR LYS LEU THR MET LEU GLU ILE
SEQRES 16 A 475 TYR LYS HIS PHE ASN LEU CYS GLN LEU THR ILE ASP PHE
SEQRES 17 A 475 LEU GLY HIS ALA VAL ALA LEU TYR LEU ASN ASP ASP TYR
SEQRES 18 A 475 LEU LYS GLN PRO ALA TYR LEU THR LEU GLU ARG ILE LYS
SEQRES 19 A 475 LEU TYR MET GLN SER ILE SER ALA PHE GLY LYS SER PRO
SEQRES 20 A 475 PHE ILE TYR PRO LEU TYR GLY LEU GLY GLY ILE PRO GLU
SEQRES 21 A 475 GLY PHE SER ARG MET CYS ALA ILE ASN GLY GLY THR PHE
SEQRES 22 A 475 MET LEU ASN LYS ASN VAL VAL ASP PHE VAL PHE ASP ASP
SEQRES 23 A 475 ASP ASN LYS VAL CYS GLY ILE LYS SER SER ASP GLY GLU
SEQRES 24 A 475 ILE ALA TYR CYS ASP LYS VAL ILE CYS ASP PRO SER TYR
SEQRES 25 A 475 VAL MET HIS LEU LYS ASN LYS ILE LYS LYS ILE GLY GLN
SEQRES 26 A 475 VAL ILE ARG CYS ILE CYS ILE LEU SER ASN PRO ILE PRO
SEQRES 27 A 475 GLU THR ASN GLN THR ASN SER CYS GLN ILE ILE ILE PRO
SEQRES 28 A 475 GLN ASN GLN LEU ASN ARG LYS SER ASP ILE TYR ILE ASN
SEQRES 29 A 475 LEU VAL SER PHE GLN HIS GLY VAL THR LEU LYS GLY LYS
SEQRES 30 A 475 TYR ILE ALA ILE VAL SER ALA THR VAL GLU THR ASN ASN
SEQRES 31 A 475 PRO ILE LYS GLU ILE GLU LYS PRO LEU GLU LEU LEU GLY
SEQRES 32 A 475 THR ILE GLU GLU LYS PHE VAL LYS ILE SER ASP LEU TYR
SEQRES 33 A 475 VAL SER THR SER LYS LYS PRO ALA ASP ASN ILE PHE VAL
SEQRES 34 A 475 THR SER SER TYR ASP ALA THR SER HIS PHE GLU THR ALA
SEQRES 35 A 475 THR ASN ASP LEU LEU GLN ILE TRP GLU ASN LEU TRP GLY
SEQRES 36 A 475 GLN LYS LEU ASN PHE ASP ASP LEU ASN THR ASN ALA ASP
SEQRES 37 A 475 GLY GLU ALA PRO ASP PHE ASN
FORMUL 2 HOH *215(H2 O)
HELIX 1 1 GLY A 13 TYR A 26 1 14
HELIX 2 2 GLY A 40 THR A 43 5 4
HELIX 3 3 ASN A 47 LYS A 56 1 10
HELIX 4 4 PRO A 62 GLY A 66 5 5
HELIX 5 5 GLU A 67 TRP A 71 5 5
HELIX 6 6 GLY A 84 THR A 93 1 10
HELIX 7 7 VAL A 95 LEU A 99 5 5
HELIX 8 8 THR A 130 VAL A 136 1 7
HELIX 9 9 SER A 141 TRP A 158 1 18
HELIX 10 10 LYS A 162 TRP A 166 5 5
HELIX 11 11 THR A 175 PHE A 183 1 9
HELIX 12 12 CYS A 186 VAL A 197 1 12
HELIX 13 13 ASP A 203 GLN A 208 5 6
HELIX 14 14 PRO A 209 SER A 225 1 17
HELIX 15 15 GLY A 240 ASN A 253 1 14
HELIX 16 16 PRO A 294 VAL A 297 5 4
HELIX 17 17 PRO A 335 ASN A 340 5 6
HELIX 18 18 GLN A 353 GLY A 355 5 3
HELIX 19 19 ASN A 374 ILE A 379 1 6
HELIX 20 20 ILE A 379 LEU A 385 1 7
HELIX 21 21 PHE A 423 GLY A 439 1 17
SHEET 1 A 6 PHE A 257 MET A 258 0
SHEET 2 A 6 ILE A 30 LEU A 33 1 N VAL A 32 O MET A 258
SHEET 3 A 6 HIS A 4 LEU A 10 1 N ILE A 9 O LEU A 31
SHEET 4 A 6 ILE A 284 CYS A 292 1 O ILE A 291 N LEU A 10
SHEET 5 A 6 VAL A 274 SER A 279 -1 N ILE A 277 O ALA A 285
SHEET 6 A 6 VAL A 263 PHE A 268 -1 N VAL A 267 O CYS A 275
SHEET 1 B 5 PHE A 257 MET A 258 0
SHEET 2 B 5 ILE A 30 LEU A 33 1 N VAL A 32 O MET A 258
SHEET 3 B 5 HIS A 4 LEU A 10 1 N ILE A 9 O LEU A 31
SHEET 4 B 5 ILE A 284 CYS A 292 1 O ILE A 291 N LEU A 10
SHEET 5 B 5 ILE A 411 VAL A 413 1 O PHE A 412 N VAL A 290
SHEET 1 C 2 SER A 45 LEU A 46 0
SHEET 2 C 2 VAL A 73 ASP A 74 -1 O VAL A 73 N LEU A 46
SHEET 1 D 3 ILE A 80 LEU A 81 0
SHEET 2 D 3 PHE A 232 PRO A 235 -1 O ILE A 233 N ILE A 80
SHEET 3 D 3 TRP A 101 VAL A 103 -1 N LEU A 102 O TYR A 234
SHEET 1 E 7 LYS A 122 LYS A 126 0
SHEET 2 E 7 GLY A 106 GLN A 113 -1 N GLN A 113 O LYS A 122
SHEET 3 E 7 CYS A 330 ILE A 334 1 O GLN A 331 N TYR A 108
SHEET 4 E 7 ILE A 345 SER A 351 -1 O ILE A 345 N ILE A 334
SHEET 5 E 7 TYR A 362 THR A 369 -1 O ILE A 363 N VAL A 350
SHEET 6 E 7 ILE A 304 LEU A 317 -1 N LEU A 317 O TYR A 362
SHEET 7 E 7 ILE A 389 SER A 402 -1 O LEU A 399 N ILE A 307
CRYST1 80.885 116.565 125.916 90.00 90.00 90.00 C 2 2 21 8
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 0.012363 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007942 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
