HEADER TRANSFERASE 28-MAR-07 2PBF
TITLE CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-L-ISOASPARTATE O-
TITLE 2 METHYLTRANSFERASE BETA-ASPARTATE METHYLTRANSFERASE (PCMT) FROM
TITLE 3 PLASMODIUM FALCIPARUM IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE BETA-ASPARTATE
COMPND 3 METHYLTRANSFERASE;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: RESIDUES 15-240;
COMPND 6 EC: 2.1.1.77;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 GENE: PF14_0309;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15-LIC
KEYWDS METHYLTRANSFERASE, PROTEIN REPAIR, ISOASPARTYL FORMATION, P.
KEYWDS 2 FALCIPARUM, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,A.HASSANALI,L.LIN,J.LEW,Y.ZHAO,M.RAVICHANDRAN,G.WASNEY,
AUTHOR 2 M.VEDADI,I.KOZIERADZKI,A.BOCHKAREV,A.M.EDWARDS,C.H.ARROWSMITH,
AUTHOR 3 J.WEIGELT,M.SUNDSTROM,R.HUI,W.QIU,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 4 (SGC)
REVDAT 5 30-AUG-23 2PBF 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2PBF 1 REMARK
REVDAT 3 13-JUL-11 2PBF 1 VERSN
REVDAT 2 24-FEB-09 2PBF 1 VERSN
REVDAT 1 10-APR-07 2PBF 0
JRNL AUTH A.K.WERNIMONT,A.HASSANALI,L.LIN,J.LEW,Y.ZHAO,M.RAVICHANDRAN,
JRNL AUTH 2 G.WASNEY,M.VEDADI,I.KOZIERADZKI,A.BOCHKAREV,A.M.EDWARDS,
JRNL AUTH 3 C.H.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,R.HUI,W.QIU
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-L-ISOASPARTATE
JRNL TITL 2 O-METHYLTRANSFERASE BETA-ASPARTATE METHYLTRANSFERASE (PCMT)
JRNL TITL 3 FROM PLASMODIUM FALCIPARUM IN COMPLEX WITH
JRNL TITL 4 S-ADENOSYL-L-HOMOCYSTEINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 31337
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1673
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2278
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3476
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.46000
REMARK 3 B22 (A**2) : 1.46000
REMARK 3 B33 (A**2) : -2.19000
REMARK 3 B12 (A**2) : 0.73000
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): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.188
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.398
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3582 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4832 ; 1.503 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 432 ; 6.484 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 154 ;38.433 ;25.325
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 696 ;16.646 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;23.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 566 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2580 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1845 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2434 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 229 ; 0.175 ; 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): 18 ; 0.243 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.126 ; 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): 2246 ; 0.761 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3540 ; 1.309 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1502 ; 1.906 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1292 ; 2.870 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 9 A 227 5
REMARK 3 1 B 9 B 227 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 872 ; 0.05 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 863 ; 0.24 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 872 ; 0.29 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 863 ; 0.78 ; 10.00
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 : 1.40
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
REMARK 4
REMARK 4 2PBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042191.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33234
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.89900
REMARK 200 R SYM FOR SHELL (I) : 0.71300
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 1L1N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M
REMARK 280 HEPES PH 7.2, 2 MM SAH, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,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 51.59267
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 25.79633
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS A MONOMER.
REMARK 300 SEE REMARK 350 FOR INFORMATION ON GENERATING THE
REMARK 300 BIOLOGICAL MOLECULE(S).
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 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 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 MET A 4
REMARK 465 TYR A 5
REMARK 465 LYS A 6
REMARK 465 LEU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 210
REMARK 465 GLY B 1
REMARK 465 ASN B 2
REMARK 465 ASN B 3
REMARK 465 MET B 4
REMARK 465 TYR B 5
REMARK 465 LYS B 6
REMARK 465 LEU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 210
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 155 CD OE1 OE2
REMARK 470 ASP A 196 CG OD1 OD2
REMARK 470 GLU B 159 CD OE1 OE2
REMARK 470 ASP B 196 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 O HOH A 384 O HOH A 388 2.10
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 LEU A 189 CA - CB - CG ANGL. DEV. = 15.3 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 ILE A 46 60.84 23.56
REMARK 500 ILE A 55 -66.65 -104.27
REMARK 500 SER A 56 166.67 175.81
REMARK 500 ASN A 186 -1.53 73.06
REMARK 500 ASP A 196 -101.31 54.67
REMARK 500 ASN A 208 -69.68 -134.59
REMARK 500 LEU A 216 -79.86 -90.05
REMARK 500 ILE B 46 60.86 26.53
REMARK 500 ILE B 55 -68.44 -104.37
REMARK 500 SER B 56 165.79 176.00
REMARK 500 GLU B 194 109.77 -53.06
REMARK 500 ASP B 196 -102.95 57.68
REMARK 500 ASN B 208 -78.47 -129.08
REMARK 500 LEU B 216 -77.26 -93.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 207 ASN A 208 148.48
REMARK 500 LYS B 207 ASN B 208 143.38
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 SAH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 301
DBREF 2PBF A 2 227 UNP Q8ILD5 Q8ILD5_PLAF7 15 240
DBREF 2PBF B 2 227 UNP Q8ILD5 Q8ILD5_PLAF7 15 240
SEQADV 2PBF GLY A 1 UNP Q8ILD5 CLONING ARTIFACT
SEQADV 2PBF GLY B 1 UNP Q8ILD5 CLONING ARTIFACT
SEQRES 1 A 227 GLY ASN ASN MET TYR LYS LEU SER GLU ASN ASN HIS LYS
SEQRES 2 A 227 SER LEU LEU GLU ASN LEU LYS ARG ARG GLY ILE ILE ASP
SEQRES 3 A 227 ASP ASP ASP VAL TYR ASN THR MET LEU GLN VAL ASP ARG
SEQRES 4 A 227 GLY LYS TYR ILE LYS GLU ILE PRO TYR ILE ASP THR PRO
SEQRES 5 A 227 VAL TYR ILE SER HIS GLY VAL THR ILE SER ALA PRO HIS
SEQRES 6 A 227 MET HIS ALA LEU SER LEU LYS ARG LEU ILE ASN VAL LEU
SEQRES 7 A 227 LYS PRO GLY SER ARG ALA ILE ASP VAL GLY SER GLY SER
SEQRES 8 A 227 GLY TYR LEU THR VAL CYS MET ALA ILE LYS MET ASN VAL
SEQRES 9 A 227 LEU GLU ASN LYS ASN SER TYR VAL ILE GLY LEU GLU ARG
SEQRES 10 A 227 VAL LYS ASP LEU VAL ASN PHE SER LEU GLU ASN ILE LYS
SEQRES 11 A 227 ARG ASP LYS PRO GLU LEU LEU LYS ILE ASP ASN PHE LYS
SEQRES 12 A 227 ILE ILE HIS LYS ASN ILE TYR GLN VAL ASN GLU GLU GLU
SEQRES 13 A 227 LYS LYS GLU LEU GLY LEU PHE ASP ALA ILE HIS VAL GLY
SEQRES 14 A 227 ALA SER ALA SER GLU LEU PRO GLU ILE LEU VAL ASP LEU
SEQRES 15 A 227 LEU ALA GLU ASN GLY LYS LEU ILE ILE PRO ILE GLU GLU
SEQRES 16 A 227 ASP TYR THR GLN VAL LEU TYR GLU ILE THR LYS LYS ASN
SEQRES 17 A 227 GLY LYS ILE ILE LYS ASP ARG LEU PHE ASP VAL CYS PHE
SEQRES 18 A 227 VAL SER LEU LYS LYS ASN
SEQRES 1 B 227 GLY ASN ASN MET TYR LYS LEU SER GLU ASN ASN HIS LYS
SEQRES 2 B 227 SER LEU LEU GLU ASN LEU LYS ARG ARG GLY ILE ILE ASP
SEQRES 3 B 227 ASP ASP ASP VAL TYR ASN THR MET LEU GLN VAL ASP ARG
SEQRES 4 B 227 GLY LYS TYR ILE LYS GLU ILE PRO TYR ILE ASP THR PRO
SEQRES 5 B 227 VAL TYR ILE SER HIS GLY VAL THR ILE SER ALA PRO HIS
SEQRES 6 B 227 MET HIS ALA LEU SER LEU LYS ARG LEU ILE ASN VAL LEU
SEQRES 7 B 227 LYS PRO GLY SER ARG ALA ILE ASP VAL GLY SER GLY SER
SEQRES 8 B 227 GLY TYR LEU THR VAL CYS MET ALA ILE LYS MET ASN VAL
SEQRES 9 B 227 LEU GLU ASN LYS ASN SER TYR VAL ILE GLY LEU GLU ARG
SEQRES 10 B 227 VAL LYS ASP LEU VAL ASN PHE SER LEU GLU ASN ILE LYS
SEQRES 11 B 227 ARG ASP LYS PRO GLU LEU LEU LYS ILE ASP ASN PHE LYS
SEQRES 12 B 227 ILE ILE HIS LYS ASN ILE TYR GLN VAL ASN GLU GLU GLU
SEQRES 13 B 227 LYS LYS GLU LEU GLY LEU PHE ASP ALA ILE HIS VAL GLY
SEQRES 14 B 227 ALA SER ALA SER GLU LEU PRO GLU ILE LEU VAL ASP LEU
SEQRES 15 B 227 LEU ALA GLU ASN GLY LYS LEU ILE ILE PRO ILE GLU GLU
SEQRES 16 B 227 ASP TYR THR GLN VAL LEU TYR GLU ILE THR LYS LYS ASN
SEQRES 17 B 227 GLY LYS ILE ILE LYS ASP ARG LEU PHE ASP VAL CYS PHE
SEQRES 18 B 227 VAL SER LEU LYS LYS ASN
HET SAH A 301 26
HET SAH B 301 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 5 HOH *181(H2 O)
HELIX 1 1 ASN A 11 ARG A 22 1 12
HELIX 2 2 ASP A 27 GLN A 36 1 10
HELIX 3 3 VAL A 37 TYR A 42 5 6
HELIX 4 4 ALA A 63 ILE A 75 1 13
HELIX 5 5 GLY A 92 MET A 102 1 11
HELIX 6 6 VAL A 118 LYS A 133 1 16
HELIX 7 7 PRO A 134 LYS A 138 5 5
HELIX 8 8 ASN A 148 VAL A 152 5 5
HELIX 9 9 ASN A 153 GLY A 161 1 9
HELIX 10 10 PRO A 176 LEU A 182 1 7
HELIX 11 11 ASN B 11 ARG B 22 1 12
HELIX 12 12 ASP B 27 GLN B 36 1 10
HELIX 13 13 VAL B 37 TYR B 42 5 6
HELIX 14 14 ALA B 63 ILE B 75 1 13
HELIX 15 15 GLY B 92 MET B 102 1 11
HELIX 16 16 VAL B 118 LYS B 133 1 16
HELIX 17 17 PRO B 134 ILE B 139 5 6
HELIX 18 18 ASN B 148 VAL B 152 5 5
HELIX 19 19 ASN B 153 GLY B 161 1 9
HELIX 20 20 PRO B 176 LEU B 182 1 7
SHEET 1 A 2 VAL A 53 SER A 56 0
SHEET 2 A 2 VAL A 59 ILE A 61 -1 O VAL A 59 N ILE A 55
SHEET 1 B 7 PHE A 142 HIS A 146 0
SHEET 2 B 7 TYR A 111 GLU A 116 1 N GLY A 114 O ILE A 145
SHEET 3 B 7 ARG A 83 VAL A 87 1 N ASP A 86 O LEU A 115
SHEET 4 B 7 PHE A 163 VAL A 168 1 O HIS A 167 N VAL A 87
SHEET 5 B 7 LEU A 183 GLU A 195 1 O ILE A 190 N ILE A 166
SHEET 6 B 7 THR A 198 THR A 205 -1 O ILE A 204 N LEU A 189
SHEET 7 B 7 ILE A 212 VAL A 219 -1 O VAL A 219 N GLN A 199
SHEET 1 C 2 VAL B 53 SER B 56 0
SHEET 2 C 2 VAL B 59 ILE B 61 -1 O VAL B 59 N ILE B 55
SHEET 1 D 7 PHE B 142 HIS B 146 0
SHEET 2 D 7 TYR B 111 GLU B 116 1 N GLY B 114 O ILE B 145
SHEET 3 D 7 ARG B 83 VAL B 87 1 N ALA B 84 O TYR B 111
SHEET 4 D 7 PHE B 163 VAL B 168 1 O HIS B 167 N VAL B 87
SHEET 5 D 7 LEU B 183 GLU B 195 1 O ILE B 190 N ILE B 166
SHEET 6 D 7 THR B 198 THR B 205 -1 O ILE B 204 N LEU B 189
SHEET 7 D 7 ILE B 212 VAL B 219 -1 O VAL B 219 N GLN B 199
SITE 1 AC1 24 VAL A 59 THR A 60 ILE A 61 SER A 62
SITE 2 AC1 24 HIS A 67 GLY A 88 SER A 89 GLY A 90
SITE 3 AC1 24 SER A 91 GLU A 116 ARG A 117 VAL A 118
SITE 4 AC1 24 LYS A 147 ASN A 148 ILE A 149 GLY A 169
SITE 5 AC1 24 VAL A 222 SER A 223 LEU A 224 LYS A 225
SITE 6 AC1 24 HOH A 305 HOH A 315 HOH A 319 HOH A 379
SITE 1 AC2 24 VAL B 59 THR B 60 ILE B 61 SER B 62
SITE 2 AC2 24 HIS B 67 GLY B 88 SER B 89 GLY B 90
SITE 3 AC2 24 SER B 91 GLU B 116 ARG B 117 VAL B 118
SITE 4 AC2 24 LYS B 147 ASN B 148 ILE B 149 GLY B 169
SITE 5 AC2 24 VAL B 222 SER B 223 LEU B 224 LYS B 225
SITE 6 AC2 24 HOH B 307 HOH B 317 HOH B 321 HOH B 379
CRYST1 75.156 75.156 77.389 90.00 90.00 120.00 P 32 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013306 0.007682 0.000000 0.00000
SCALE2 0.000000 0.015364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012922 0.00000
(ATOM LINES ARE NOT SHOWN.)
END