HEADER RNA BINDING PROTEIN 24-OCT-07 3B4D
TITLE CRYSTAL STRUCTURE OF HUMAN PABPN1 RRM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYADENYLATE-BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 167-254;
COMPND 5 SYNONYM: POLY(A)-BINDING PROTEIN 2, POLY(A)-BINDING PROTEIN II,
COMPND 6 PABII, POLYADENYLATE-BINDING NUCLEAR PROTEIN 1, NUCLEAR POLY(A)-
COMPND 7 BINDING PROTEIN 1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PABPN1, PAB2, PABP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS RRM FOLD, ALPHA-BETA SANDWICH STRUCTURE, RNA BINDING DOMAIN, RNA
KEYWDS 2 RECOGNITION MOTIF, ACETYLATION, ALTERNATIVE SPLICING, COILED COIL,
KEYWDS 3 CYTOPLASM, DISEASE MUTATION, METHYLATION, MRNA PROCESSING, NUCLEUS,
KEYWDS 4 POLYMORPHISM, RNA-BINDING, TRIPLET REPEAT EXPANSION, RNA BINDING
KEYWDS 5 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.GE,S.TONG,M.TENG,L.NIU
REVDAT 4 13-MAR-24 3B4D 1 SEQADV
REVDAT 3 24-FEB-09 3B4D 1 VERSN
REVDAT 2 08-APR-08 3B4D 1 JRNL
REVDAT 1 15-JAN-08 3B4D 0
JRNL AUTH H.GE,D.ZHOU,S.TONG,Y.GAO,M.TENG,L.NIU
JRNL TITL CRYSTAL STRUCTURE AND POSSIBLE DIMERIZATION OF THE SINGLE
JRNL TITL 2 RRM OF HUMAN PABPN1
JRNL REF PROTEINS V. 71 1539 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18275081
JRNL DOI 10.1002/PROT.21973
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 8561
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 425
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) : 631
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 625
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.789
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 637 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 856 ; 1.312 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 79 ; 5.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 31 ;35.356 ;22.581
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 108 ;13.623 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;18.896 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 92 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 487 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 248 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 435 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 62 ; 0.172 ; 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): 30 ; 0.192 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.250 ; 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): 408 ; 1.051 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 629 ; 1.716 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 255 ; 2.775 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 227 ; 4.300 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3B4D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000045063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : AUTOMAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.001
REMARK 200 RESOLUTION RANGE LOW (A) : 65.233
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 4.2M SODIUM CHLORIDE,
REMARK 280 PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 46.17300
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 46.17300
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 46.17300
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 46.17300
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 46.17300
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 46.17300
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: 1540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.7 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 BIOMT1 2 -1.000000 0.000000 0.000000 92.34600
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 167
REMARK 465 GLU A 168
REMARK 465 THR A 249
REMARK 465 ASN A 250
REMARK 465 ARG A 251
REMARK 465 PRO A 252
REMARK 465 GLY A 253
REMARK 465 ILE A 254
REMARK 465 LEU A 255
REMARK 465 GLU A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
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 ASN A 178 50.01 72.65
REMARK 500 GLU A 234 -2.97 72.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B4M RELATED DB: PDB
DBREF 3B4D A 167 254 UNP Q86U42 PABP2_HUMAN 167 254
SEQADV 3B4D LEU A 255 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D GLU A 256 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 257 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 258 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 259 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 260 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 261 UNP Q86U42 EXPRESSION TAG
SEQADV 3B4D HIS A 262 UNP Q86U42 EXPRESSION TAG
SEQRES 1 A 96 MET GLU ALA ASP ALA ARG SER ILE TYR VAL GLY ASN VAL
SEQRES 2 A 96 ASP TYR GLY ALA THR ALA GLU GLU LEU GLU ALA HIS PHE
SEQRES 3 A 96 HIS GLY CYS GLY SER VAL ASN ARG VAL THR ILE LEU CYS
SEQRES 4 A 96 ASP LYS PHE SER GLY HIS PRO LYS GLY PHE ALA TYR ILE
SEQRES 5 A 96 GLU PHE SER ASP LYS GLU SER VAL ARG THR SER LEU ALA
SEQRES 6 A 96 LEU ASP GLU SER LEU PHE ARG GLY ARG GLN ILE LYS VAL
SEQRES 7 A 96 ILE PRO LYS ARG THR ASN ARG PRO GLY ILE LEU GLU HIS
SEQRES 8 A 96 HIS HIS HIS HIS HIS
FORMUL 2 HOH *97(H2 O)
HELIX 1 1 ALA A 169 ALA A 171 5 3
HELIX 2 2 THR A 184 HIS A 193 1 10
HELIX 3 3 GLY A 194 GLY A 196 5 3
HELIX 4 4 LYS A 223 LEU A 230 1 8
HELIX 5 5 ALA A 231 ASP A 233 5 3
SHEET 1 A 4 VAL A 198 CYS A 205 0
SHEET 2 A 4 GLY A 214 PHE A 220 -1 O GLU A 219 N ASN A 199
SHEET 3 A 4 SER A 173 GLY A 177 -1 N VAL A 176 O ALA A 216
SHEET 4 A 4 LYS A 243 PRO A 246 -1 O LYS A 243 N GLY A 177
SHEET 1 B 2 LEU A 236 PHE A 237 0
SHEET 2 B 2 ARG A 240 GLN A 241 -1 O ARG A 240 N PHE A 237
CRYST1 92.346 92.346 92.346 90.00 90.00 90.00 I 2 3 24
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 0.010829 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010829 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010829 0.00000
(ATOM LINES ARE NOT SHOWN.)
END