HEADER HYDROLASE 23-OCT-13 4NBI
TITLE D-AMINOACYL-TRNA DEACYLASE (DTD) FROM PLASMODIUM FALCIPARUM IN COMPLEX
TITLE 2 WITH D-TYROSYL-3'-AMINOADENOSINE AT 1.86 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-TYROSYL-TRNA(TYR) DEACYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 GENE: DTD, PF11_0095;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21B
KEYWDS DTD, DEACYLASE, DTD-LIKE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AHMAD,S.B.ROUTH,V.KAMARTHAPU,R.SANKARANARAYANAN
REVDAT 3 08-NOV-23 4NBI 1 REMARK
REVDAT 2 15-NOV-17 4NBI 1 REMARK
REVDAT 1 18-DEC-13 4NBI 0
JRNL AUTH S.AHMAD,S.B.ROUTH,V.KAMARTHAPU,J.CHALISSERY,S.MUTHUKUMAR,
JRNL AUTH 2 T.HUSSAIN,S.P.KRUPARANI,M.V.DESHMUKH,R.SANKARANARAYANAN
JRNL TITL MECHANISM OF CHIRAL PROOFREADING DURING TRANSLATION OF THE
JRNL TITL 2 GENETIC CODE.
JRNL REF ELIFE V. 2 01519 2013
JRNL REFN ESSN 2050-084X
JRNL PMID 24302572
JRNL DOI 10.7554/ELIFE.01519
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 25154
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1276
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1619
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.71000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -1.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.651
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2693 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3633 ; 1.093 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 311 ; 5.891 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;45.213 ;25.504
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 501 ;12.881 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.760 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 402 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1992 ; 0.004 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES
REMARK 4
REMARK 4 4NBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000082993.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25156
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.28300
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, PHASER
REMARK 200 STARTING MODEL: 3KNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 3350, 0.6M SODIUM CHLORIDE,
REMARK 280 0.1M HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 41.06700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.87150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.06700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.87150
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 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 LYS A 164
REMARK 465 GLU B 18
REMARK 465 ASN B 19
REMARK 465 ILE B 20
REMARK 465 GLY B 21
REMARK 465 GLU B 22
REMARK 465 ASN B 23
REMARK 465 GLU B 24
REMARK 465 LYS B 25
REMARK 465 GLU B 26
REMARK 465 ASN B 161
REMARK 465 LEU B 162
REMARK 465 ASN B 163
REMARK 465 LYS B 164
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 GLU A 28 CB CG CD OE1 OE2
REMARK 480 GLU A 32 CD OE1 OE2
REMARK 480 LYS A 34 CE NZ
REMARK 480 LYS A 45 CE NZ
REMARK 480 ASN A 69 CB CG OD1 ND2
REMARK 480 ASN B 94 CG OD1 ND2
REMARK 480 LYS B 97 CD CE NZ
REMARK 480 ASP B 102 CB CG OD1 OD2
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 GLU A 32 CG GLU A 32 CD -0.109
REMARK 500 ASN A 69 CA ASN A 69 CB 0.182
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 ASN A 69 N - CA - CB ANGL. DEV. = -27.7 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 LYS A 34 -135.58 -94.08
REMARK 500 ASN A 67 -113.13 -92.46
REMARK 500 TYR A 127 -109.41 -117.47
REMARK 500 LYS B 34 -134.63 -94.71
REMARK 500 PHE B 92 65.31 -110.12
REMARK 500 PHE B 103 42.05 -97.04
REMARK 500 TYR B 127 -113.51 -114.51
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 D3Y A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3Y B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NBJ RELATED DB: PDB
DBREF 4NBI A 1 164 UNP Q8IIS0 Q8IIS0_PLAF7 1 164
DBREF 4NBI B 1 164 UNP Q8IIS0 Q8IIS0_PLAF7 1 164
SEQRES 1 A 164 MET ARG VAL VAL ILE GLN ARG VAL LYS GLY ALA ILE LEU
SEQRES 2 A 164 SER VAL ARG LYS GLU ASN ILE GLY GLU ASN GLU LYS GLU
SEQRES 3 A 164 LEU GLU ILE ILE SER GLU ILE LYS ASN GLY LEU ILE CYS
SEQRES 4 A 164 PHE LEU GLY ILE HIS LYS ASN ASP THR TRP GLU ASP ALA
SEQRES 5 A 164 LEU TYR ILE ILE ARG LYS CYS LEU ASN LEU ARG LEU TRP
SEQRES 6 A 164 ASN ASN ASP ASN LYS THR TRP ASP LYS ASN VAL LYS ASP
SEQRES 7 A 164 LEU ASN TYR GLU LEU LEU ILE VAL SER GLN PHE THR LEU
SEQRES 8 A 164 PHE GLY ASN THR LYS LYS GLY ASN LYS PRO ASP PHE HIS
SEQRES 9 A 164 LEU ALA LYS GLU PRO ASN GLU ALA LEU ILE PHE TYR ASN
SEQRES 10 A 164 LYS ILE ILE ASP GLU PHE LYS LYS GLN TYR ASN ASP ASP
SEQRES 11 A 164 LYS ILE LYS ILE GLY LYS PHE GLY ASN TYR MET ASN ILE
SEQRES 12 A 164 ASP VAL THR ASN ASP GLY PRO VAL THR ILE TYR ILE ASP
SEQRES 13 A 164 THR HIS ASP ILE ASN LEU ASN LYS
SEQRES 1 B 164 MET ARG VAL VAL ILE GLN ARG VAL LYS GLY ALA ILE LEU
SEQRES 2 B 164 SER VAL ARG LYS GLU ASN ILE GLY GLU ASN GLU LYS GLU
SEQRES 3 B 164 LEU GLU ILE ILE SER GLU ILE LYS ASN GLY LEU ILE CYS
SEQRES 4 B 164 PHE LEU GLY ILE HIS LYS ASN ASP THR TRP GLU ASP ALA
SEQRES 5 B 164 LEU TYR ILE ILE ARG LYS CYS LEU ASN LEU ARG LEU TRP
SEQRES 6 B 164 ASN ASN ASP ASN LYS THR TRP ASP LYS ASN VAL LYS ASP
SEQRES 7 B 164 LEU ASN TYR GLU LEU LEU ILE VAL SER GLN PHE THR LEU
SEQRES 8 B 164 PHE GLY ASN THR LYS LYS GLY ASN LYS PRO ASP PHE HIS
SEQRES 9 B 164 LEU ALA LYS GLU PRO ASN GLU ALA LEU ILE PHE TYR ASN
SEQRES 10 B 164 LYS ILE ILE ASP GLU PHE LYS LYS GLN TYR ASN ASP ASP
SEQRES 11 B 164 LYS ILE LYS ILE GLY LYS PHE GLY ASN TYR MET ASN ILE
SEQRES 12 B 164 ASP VAL THR ASN ASP GLY PRO VAL THR ILE TYR ILE ASP
SEQRES 13 B 164 THR HIS ASP ILE ASN LEU ASN LYS
HET D3Y A 201 31
HET PGE A 502 10
HET D3Y B 201 31
HETNAM D3Y 3'-DEOXY-3'-(D-TYROSYLAMINO)ADENOSINE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 D3Y 2(C19 H23 N7 O5)
FORMUL 4 PGE C6 H14 O4
FORMUL 6 HOH *250(H2 O)
HELIX 1 1 THR A 48 LEU A 62 1 15
HELIX 2 2 PHE A 89 GLY A 93 5 5
HELIX 3 3 GLU A 108 TYR A 127 1 20
HELIX 4 4 ASN A 128 ASP A 130 5 3
HELIX 5 5 HIS A 158 ILE A 160 5 3
HELIX 6 6 THR B 48 LEU B 62 1 15
HELIX 7 7 PHE B 89 GLY B 93 5 5
HELIX 8 8 GLU B 108 TYR B 127 1 20
HELIX 9 9 ASN B 128 ASP B 130 5 3
SHEET 1 A 6 LEU A 27 ILE A 33 0
SHEET 2 A 6 ARG A 2 ARG A 16 -1 N LEU A 13 O SER A 31
SHEET 3 A 6 MET A 141 ASP A 156 -1 O ASN A 142 N SER A 14
SHEET 4 A 6 MET B 141 ASP B 156 -1 O ILE B 143 N ASN A 147
SHEET 5 A 6 ARG B 2 VAL B 15 -1 N ILE B 5 O ILE B 153
SHEET 6 A 6 GLU B 28 ILE B 33 -1 O SER B 31 N LEU B 13
SHEET 1 B10 ILE A 132 ILE A 134 0
SHEET 2 B10 GLU A 82 SER A 87 1 N LEU A 83 O LYS A 133
SHEET 3 B10 GLY A 36 GLY A 42 1 N CYS A 39 O LEU A 84
SHEET 4 B10 ARG A 2 ARG A 16 -1 N ARG A 2 O GLY A 42
SHEET 5 B10 MET A 141 ASP A 156 -1 O ASN A 142 N SER A 14
SHEET 6 B10 MET B 141 ASP B 156 -1 O ILE B 143 N ASN A 147
SHEET 7 B10 ARG B 2 VAL B 15 -1 N ILE B 5 O ILE B 153
SHEET 8 B10 GLY B 36 GLY B 42 -1 O GLY B 42 N ARG B 2
SHEET 9 B10 GLU B 82 SER B 87 1 O VAL B 86 N CYS B 39
SHEET 10 B10 ILE B 132 ILE B 134 1 O LYS B 133 N LEU B 83
CISPEP 1 GLY A 149 PRO A 150 0 -9.78
CISPEP 2 GLY B 149 PRO B 150 0 -11.02
SITE 1 AC1 14 LEU A 41 ILE A 43 SER A 87 GLN A 88
SITE 2 AC1 14 PHE A 89 LYS A 107 ALA A 112 PHE A 137
SITE 3 AC1 14 GLY A 138 ASN A 139 HOH A 648 HOH A 705
SITE 4 AC1 14 GLY B 149 PRO B 150
SITE 1 AC2 5 ASP A 144 THR A 146 GLY B 10 ILE B 12
SITE 2 AC2 5 THR B 146
SITE 1 AC3 15 GLY A 149 PRO A 150 LEU B 41 ILE B 43
SITE 2 AC3 15 SER B 87 GLN B 88 PHE B 89 LYS B 107
SITE 3 AC3 15 PHE B 137 GLY B 138 ASN B 139 HOH B 343
SITE 4 AC3 15 HOH B 345 HOH B 368 HOH B 393
CRYST1 82.134 65.743 56.917 90.00 93.30 90.00 C 1 2 1 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 0.012175 0.000000 0.000702 0.00000
SCALE2 0.000000 0.015211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017599 0.00000
(ATOM LINES ARE NOT SHOWN.)
END